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Volumn 78, Issue 2, 2014, Pages 231-256

The bacterial phosphoenolpyruvate: Carbohydrate phosphotransferase system: Regulation by protein phosphorylation and phosphorylation-dependent protein-protein interactions

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE PHOSPHOTRANSFERASE; CARRIER PROTEIN; HPR DOMAIN CONTAINING PROTEIN; LACS PROTEIN; PHOSPHOENOLPYRUVATE; PHOSPHOTRANSFERASE; POTASSIUM; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; PROTEIN BINDING;

EID: 84901013706     PISSN: 10922172     EISSN: 10985557     Source Type: Journal    
DOI: 10.1128/MMBR.00001-14     Document Type: Review
Times cited : (325)

References (221)
  • 1
    • 33845626641 scopus 로고    scopus 로고
    • How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria
    • Deutscher J, Francke C, Postma PW. 2006. How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria. Microbiol. Mol. Biol. Rev. 70:939-1031. http://dx.doi .org/10.1128/MMBR.00024-06.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 939-1031
    • Deutscher, J.1    Francke, C.2    Postma, P.W.3
  • 2
    • 84878273712 scopus 로고    scopus 로고
    • The bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS): An interface between energy and signal transduction
    • Erni B. 2013. The bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS): an interface between energy and signal transduction. J. Iran. Chem. Soc. 10:593-630. http://dx.doi.org/10.1007/s13738-012-0185-1.
    • (2013) J. Iran. Chem. Soc. , vol.10 , pp. 593-630
    • Erni, B.1
  • 3
    • 84863998593 scopus 로고    scopus 로고
    • Fructose degradation in the haloarchaeon Haloferax volcanii involves a bacterial type phosphoenolpyruvate- dependent phosphotransferase system, fructose-1-phosphate kinase, and class II fructose-1,6-bisphosphate aldolase
    • Pickl A, Johnsen U, Schönheit P. 2012. Fructose degradation in the haloarchaeon Haloferax volcanii involves a bacterial type phosphoenolpyruvate- dependent phosphotransferase system, fructose-1-phosphate kinase, and class II fructose-1,6-bisphosphate aldolase. J. Bacteriol. 194: 3088-3097. http://dx.doi.org/10.1128/JB.00200-12.
    • (2012) J. Bacteriol. , vol.194 , pp. 3088-3097
    • Pickl, A.1    Johnsen, U.2    Schönheit, P.3
  • 4
    • 0036217950 scopus 로고    scopus 로고
    • Regulation of gene expression in the PTS in Escherichia coli: The role and interactions of Mlc
    • Plumbridge J. 2002. Regulation of gene expression in the PTS in Escherichia coli: the role and interactions of Mlc. Curr. Opin. Microbiol. 5:187-193. http://dx.doi.org/10.1016/S1369-5274(02)00296-5.
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 187-193
    • Plumbridge, J.1
  • 5
    • 0025679385 scopus 로고
    • Domain shuffling during evolution of the proteins of the bacterial phosphotransferase system
    • Saier MH, Jr, Reizer J. 1990. Domain shuffling during evolution of the proteins of the bacterial phosphotransferase system. Res. Microbiol. 141: 1033-1038. http://dx.doi.org/10.1016/0923-2508(90)90077-4.
    • (1990) Res. Microbiol. , vol.141 , pp. 1033-1038
    • Saier Jr., M.H.1    Reizer, J.2
  • 6
    • 29144518548 scopus 로고    scopus 로고
    • Comparative genomic analyses of the bacterial phosphotransferase system
    • Barabote RD, Saier MH, Jr. 2005. Comparative genomic analyses of the bacterial phosphotransferase system. Microbiol. Mol. Biol. Rev. 69:608-634. http://dx.doi.org/10.1128/MMBR.69.4.608-634.2005.
    • (2005) Microbiol. Mol. Biol. Rev. , vol.69 , pp. 608-634
    • Barabote, R.D.1    Saier Jr., M.H.2
  • 7
    • 0035873544 scopus 로고    scopus 로고
    • The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor
    • Gutknecht R, Beutler R, Garcia-Alles LF, Baumann U, Erni B. 2001. The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor. EMBO J. 20:2480-2486. http: //dx.doi.org/10.1093/ emboj/20.10.2480.
    • (2001) EMBO J. , vol.20 , pp. 2480-2486
    • Gutknecht, R.1    Beutler, R.2    Garcia-Alles, L.F.3    Baumann, U.4    Erni, B.5
  • 9
    • 0017364905 scopus 로고
    • The phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus aureus. 2. 1H and 31P nuclearmagnetic- resonance studies on the phosphocarrier protein HPr, phosphohistidines and phosphorylated HPr
    • Gassner M, Stehlik D, Schrecker O, Hengstenberg W, Maurer W, Rüterjans H. 1977. The phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus aureus. 2. 1H and 31P nuclearmagnetic- resonance studies on the phosphocarrier protein HPr, phosphohistidines and phosphorylated HPr. Eur. J. Biochem. 75:287-296. http://dx.doi.org/10.1111/j.1432-1033.1977. tb11528.x.
    • (1977) Eur. J. Biochem. , vol.75 , pp. 287-296
    • Gassner, M.1    Stehlik, D.2    Schrecker, O.3    Hengstenberg, W.4    Maurer, W.5    Rüterjans, H.6
  • 10
    • 0020397517 scopus 로고
    • Phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus aureus: Factor IIILac, a trimeric phospho-carrier protein that also acts as a phase transfer catalyst
    • Deutscher J, Beyreuther K, Sobek MH, Stüber K, Hengstenberg W. 1982. Phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus aureus: factor IIILac, a trimeric phospho-carrier protein that also acts as a phase transfer catalyst. Biochemistry 21:4867-4873. http://dx.doi.org/10.1021/ bi00263a006.
    • (1982) Biochemistry , vol.21 , pp. 4867-4873
    • Deutscher, J.1    Beyreuther, K.2    Sobek, M.H.3    Stüber, K.4    Hengstenberg, W.5
  • 11
    • 0021507239 scopus 로고
    • Phosphoenolpyruvate-dependent phosphorylation site in enzyme IIIglc of the Escherichia coli phosphotransferase system
    • Dörschug M, Frank R, Kalbitzer HR, Hengstenberg W, Deutscher J. 1984. Phosphoenolpyruvate-dependent phosphorylation site in enzyme IIIglc of the Escherichia coli phosphotransferase system. Eur. J. Biochem. 144:113-119. http://dx.doi.org/10.1111/j.1432-1033.1984.tb08438.x.
    • (1984) Eur. J. Biochem. , vol.144 , pp. 113-119
    • Dörschug, M.1    Frank, R.2    Kalbitzer, H.R.3    Hengstenberg, W.4    Deutscher, J.5
  • 12
    • 0023772186 scopus 로고
    • S-Phosphocysteine and phosphohistidine are intermediates in the phosphoenolpyruvate-dependent mannitol transport catalyzed by Escherichia coli EIIMtl
    • Pas HH, Robillard GT. 1988. S-Phosphocysteine and phosphohistidine are intermediates in the phosphoenolpyruvate-dependent mannitol transport catalyzed by Escherichia coli EIIMtl. Biochemistry 27:5835-5839. http://dx.doi.org/10. 1021/bi00416a002.
    • (1988) Biochemistry , vol.27 , pp. 5835-5839
    • Pas, H.H.1    Robillard, G.T.2
  • 13
    • 0031046651 scopus 로고    scopus 로고
    • Protein phosphorylation chain of a Bacillus subtilis fructose-specific phosphotransferase system and its participation in regulation of the expression of the lev operon
    • Charrier V, Deutscher J, Galinier A, Martin-Verstraete I. 1997. Protein phosphorylation chain of a Bacillus subtilis fructose-specific phosphotransferase system and its participation in regulation of the expression of the lev operon. Biochemistry 36:1163-1172. http://dx.doi.org/10.1021 /bi961813w.
    • (1997) Biochemistry , vol.36 , pp. 1163-1172
    • Charrier, V.1    Deutscher, J.2    Galinier, A.3    Martin-Verstraete, I.4
  • 14
    • 84864090248 scopus 로고    scopus 로고
    • Lactobacillus casei ferments the N-Acetylglucosamine moiety of fucosyl-1,3-Nacetylglucosamine and excretes L-fucose
    • Rodríguez-Díaz J, Rubio-del-Campo A, Yebra MJ. 2012. Lactobacillus casei ferments the N-Acetylglucosamine moiety of fucosyl-1,3-Nacetylglucosamine and excretes L-fucose. Appl. Environ. Microbiol. 78: 4613-4619. http://dx.doi.org/10.1128/AEM.00474-12.
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 4613-4619
    • Rodríguez-Díaz, J.1    Rubio-Del-Campo, A.2    Yebra, M.J.3
  • 17
    • 84893354106 scopus 로고    scopus 로고
    • Analysis of the transcriptional regulator GlpR, promoter elements, and posttranscriptional processing involved in fructose- induced activation of the phosphoenolpyruvate-dependent sugar phosphotransferase system in Haloferax mediterranei
    • Cai L, Cai S, Zhao D, Wu J, Wang L, Liu X, Li M, Hou J, Zhou J, Liu J, Han J, Xiang H. 2014. Analysis of the transcriptional regulator GlpR, promoter elements, and posttranscriptional processing involved in fructose- induced activation of the phosphoenolpyruvate-dependent sugar phosphotransferase system in Haloferax mediterranei. Appl. Environ. Microbiol. 80:1430-1440. http://dx.doi.org/10.1128/AEM.03372-13.
    • (2014) Appl. Environ. Microbiol. , vol.80 , pp. 1430-1440
    • Cai, L.1    Cai, S.2    Zhao, D.3    Wu, J.4    Wang, L.5    Liu, X.6    Li, M.7    Hou, J.8    Zhou, J.9    Liu, J.10    Han, J.11    Xiang, H.12
  • 18
    • 24044461086 scopus 로고    scopus 로고
    • From ATP as substrate to ADP as coenzyme: Functional evolution of the nucleotide binding subunit of dihydroxyacetone kinase
    • Bächler C, Flükiger-Brühwiler K, Schneider P, Bähler P, Erni B. 2005. From ATP as substrate to ADP as coenzyme: functional evolution of the nucleotide binding subunit of dihydroxyacetone kinase. J. Biol. Chem. 280:18321-18325. http://dx.doi.org/10.1074/jbc.M500279200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 18321-18325
    • Bächler, C.1    Flükiger-Brühwiler, K.2    Schneider, P.3    Bähler, P.4    Erni, B.5
  • 19
    • 77958594635 scopus 로고    scopus 로고
    • Functional characterization of the incomplete phosphotransferase system (PTS) of the intracellular pathogen Brucella melitensis
    • Dozot M, Poncet S, Nicolas C, Copin R, Bouraoui H, Mazé A, Deutscher J, De Bolle X, Letesson JJ. 2010. Functional characterization of the incomplete phosphotransferase system (PTS) of the intracellular pathogen Brucella melitensis. PLoS One 5:e12679. http://dx.doi.org/10 .1371/journal.pone.0012679.
    • (2010) PLoS One , vol.5
    • Dozot, M.1    Poncet, S.2    Nicolas, C.3    Copin, R.4    Bouraoui, H.5    Mazé, A.6    Deutscher, J.7    De Bolle, X.8    Letesson, J.J.9
  • 20
    • 0000186326 scopus 로고
    • Phosphate bound to histidine in a protein as an intermediate in a novel phospho-transferase system
    • Kundig W, Ghosh S, Roseman S. 1964. Phosphate bound to histidine in a protein as an intermediate in a novel phospho-transferase system. Proc. Natl. Acad. Sci. U. S. A. 52:1067-1074. http://dx.doi.org/10.1073/pnas .52.4.1067.
    • (1964) Proc. Natl. Acad. Sci. U. S. A. , vol.52 , pp. 1067-1074
    • Kundig, W.1    Ghosh, S.2    Roseman, S.3
  • 21
    • 0020851355 scopus 로고
    • ATP-dependent protein kinasecatalyzed phosphorylation of a seryl residue in HPr, a phosphate carrier protein of the phosphotransferase system in Streptococcus pyogenes
    • Deutscher J, Saier MH, Jr. 1983. ATP-dependent protein kinasecatalyzed phosphorylation of a seryl residue in HPr, a phosphate carrier protein of the phosphotransferase system in Streptococcus pyogenes. Proc. Natl. Acad. Sci. U. S. A. 80:6790-6794. http://dx.doi.org/10.1073/pnas .80.22.6790.
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 6790-6794
    • Deutscher, J.1    Saier Jr., M.H.2
  • 23
    • 0022967087 scopus 로고
    • Phosphate transfer between acetate kinase and enzyme i of the bacterial phosphotransferase system
    • Fox DK, Meadow ND, Roseman S. 1986. Phosphate transfer between acetate kinase and enzyme I of the bacterial phosphotransferase system. J. Biol. Chem. 261:13498-13503.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13498-13503
    • Fox, D.K.1    Meadow, N.D.2    Roseman, S.3
  • 24
    • 37549052487 scopus 로고    scopus 로고
    • Genetic and proteomic analyses of a proteasome-activating nucleotidase A mutant of the haloarchaeon Haloferax volcanii
    • Kirkland PA, Gil MA, Karadzic IM, Maupin-Furlow JA. 2008. Genetic and proteomic analyses of a proteasome-activating nucleotidase A mutant of the haloarchaeon Haloferax volcanii. J. Bacteriol. 190:193-205. http://dx.doi.org/ 10.1128/JB.01196-07.
    • (2008) J. Bacteriol. , vol.190 , pp. 193-205
    • Kirkland, P.A.1    Gil, M.A.2    Karadzic, I.M.3    Maupin-Furlow, J.A.4
  • 27
    • 0027296722 scopus 로고
    • Steady state kinetics of mannitol phosphorylation catalyzed by enzyme IImtl of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system
    • Lolkema JS, ten Hoeve-Duurkens RH, Robillard GT. 1993. Steady state kinetics of mannitol phosphorylation catalyzed by enzyme IImtl of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system. J. Biol. Chem. 268:17844-17849.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17844-17849
    • Lolkema, J.S.1    Ten Hoeve-Duurkens, R.H.2    Robillard, G.T.3
  • 28
    • 0031736727 scopus 로고    scopus 로고
    • Inducer exclusion in Escherichia coli by non-PTS substrates: The role of the PEP to pyruvate ratio in determining the phosphorylation state of enzyme IIAGlc
    • Hogema BM, Arents JC, Bader R, Eijkemans K, Yoshida H, Takahashi H, Aiba H, Postma PW. 1998. Inducer exclusion in Escherichia coli by non-PTS substrates: the role of the PEP to pyruvate ratio in determining the phosphorylation state of enzyme IIAGlc. Mol. Microbiol. 30:487-498. http://dx.doi.org/10.1046/j.1365- 2958.1998.01053.x.
    • (1998) Mol. Microbiol. , vol.30 , pp. 487-498
    • Hogema, B.M.1    Arents, J.C.2    Bader, R.3    Eijkemans, K.4    Yoshida, H.5    Takahashi, H.6    Aiba, H.7    Postma, P.W.8
  • 29
  • 30
    • 0025885366 scopus 로고
    • Quantitative determination of the intracellular concentration of the various forms of HPr, a phosphocarrier protein of the phosphoenolpyruvate: Sugar phosphotransferase system in growing cells of oral streptococci
    • Vadeboncoeur C, Brochu D, Reizer J. 1991. Quantitative determination of the intracellular concentration of the various forms of HPr, a phosphocarrier protein of the phosphoenolpyruvate: sugar phosphotransferase system in growing cells of oral streptococci. Anal. Biochem. 196:24-30. http://dx.doi.org/10.1016/ 0003-2697(91)90112-7.
    • (1991) Anal. Biochem. , vol.196 , pp. 24-30
    • Vadeboncoeur, C.1    Brochu, D.2    Reizer, J.3
  • 31
    • 84891356510 scopus 로고    scopus 로고
    • HPr antagonizes the anti-70 activity of Rsd in Escherichia coli
    • Park YH, Lee CR, Choe M, Seok YJ. 2013. HPr antagonizes the anti-70 activity of Rsd in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 110: 21142-21147. http://dx.doi.org/10.1073/pnas.1316629111.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 21142-21147
    • Park, Y.H.1    Lee, C.R.2    Choe, M.3    Seok, Y.J.4
  • 32
    • 81355127364 scopus 로고    scopus 로고
    • Ketoglutarate coordinates carbon and nitrogen utilization via enzyme i inhibition
    • Doucette CD, Schwab DJ, Wingreen NS, Rabinowitz JD. 2011. Ketoglutarate coordinates carbon and nitrogen utilization via enzyme I inhibition. Nat. Chem. Biol. 7:894-901. http://dx.doi.org/10.1038 /nchembio.685.
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 894-901
    • Doucette, C.D.1    Schwab, D.J.2    Wingreen, N.S.3    Rabinowitz, J.D.4
  • 33
    • 0022979375 scopus 로고
    • Streptococcal phosphoenolpyruvate-sugar phosphotransferase system: Amino acid sequence and site of ATP-dependent phosphorylation of HPr
    • Deutscher J, Pevec B, Beyreuther K, Kiltz H-H, Hengstenberg W. 1986. Streptococcal phosphoenolpyruvate-sugar phosphotransferase system: amino acid sequence and site of ATP-dependent phosphorylation of HPr. Biochemistry 25:6543-6551. http://dx.doi.org/10.1021 /bi00369a031.
    • (1986) Biochemistry , vol.25 , pp. 6543-6551
    • Deutscher, J.1    Pevec, B.2    Beyreuther, K.3    Kiltz, H.-H.4    Hengstenberg, W.5
  • 34
    • 0000659321 scopus 로고
    • Bacterial phosphoenolpyruvate-dependent phosphotransferase system: P-Ser- HPr and its possible regulatory function
    • Deutscher J, Kessler U, Alpert CA, Hengstenberg W. 1984. Bacterial phosphoenolpyruvate-dependent phosphotransferase system: P-Ser- HPr and its possible regulatory function. Biochemistry 23:4455-4460. http://dx.doi.org/10. 1021/bi00314a033.
    • (1984) Biochemistry , vol.23 , pp. 4455-4460
    • Deutscher, J.1    Kessler, U.2    Alpert, C.A.3    Hengstenberg, W.4
  • 36
    • 0021187205 scopus 로고
    • Purification and characterization of an ATP-dependent protein kinase from Streptococcus faecalis
    • Deutscher J, Engelmann R. 1984. Purification and characterization of an ATP-dependent protein kinase from Streptococcus faecalis. FEMS Microbiol. Lett. 23:157-162. http://dx.doi.org/10.1111/j.1574-6968.1984 .tb01053.x.
    • (1984) FEMS Microbiol. Lett. , vol.23 , pp. 157-162
    • Deutscher, J.1    Engelmann, R.2
  • 37
    • 0021211416 scopus 로고
    • Properties of ATP-dependent protein kinase from Streptococcus pyogenes that phosphorylates a seryl residue in HPr, a phosphocarrier protein of the phosphotransferase system
    • Reizer J, Novotny MJ, Hengstenberg W, Saier MH, Jr. 1984. Properties of ATP-dependent protein kinase from Streptococcus pyogenes that phosphorylates a seryl residue in HPr, a phosphocarrier protein of the phosphotransferase system. J. Bacteriol. 160:333-340.
    • (1984) J. Bacteriol. , vol.160 , pp. 333-340
    • Reizer, J.1    Novotny, M.J.2    Hengstenberg, W.3    Saier Jr., M.H.4
  • 38
    • 0022623069 scopus 로고
    • Stimulation of dihydroxyacetone and glycerol kinase activity in Streptococcus faecalis by phosphoenolpyruvatedependent phosphorylation catalyzed by enzyme i and HPr of the phosphotransferase system
    • Deutscher J, Sauerwald H. 1986. Stimulation of dihydroxyacetone and glycerol kinase activity in Streptococcus faecalis by phosphoenolpyruvatedependent phosphorylation catalyzed by enzyme I and HPr of the phosphotransferase system. J. Bacteriol. 166:829-836.
    • (1986) J. Bacteriol. , vol.166 , pp. 829-836
    • Deutscher, J.1    Sauerwald, H.2
  • 39
    • 0347093516 scopus 로고    scopus 로고
    • Structures of enterococcal glycerol kinase in the absence and presence of glycerol: Correlation of conformation to substrate binding and a mechanism of activation by phosphorylation
    • Yeh JI, Charrier V, Paulo J, Hou L, Darbon E, Claiborne A, Hol WGJ, Deutscher J. 2004. Structures of enterococcal glycerol kinase in the absence and presence of glycerol: correlation of conformation to substrate binding and a mechanism of activation by phosphorylation. Biochemistry 43:362-373. http://dx.doi.org/10.1021/bi034258o.
    • (2004) Biochemistry , vol.43 , pp. 362-373
    • Yeh, J.I.1    Charrier, V.2    Paulo, J.3    Hou, L.4    Darbon, E.5    Claiborne, A.6    Hol, W.G.J.7    Deutscher, J.8
  • 40
    • 0036227754 scopus 로고    scopus 로고
    • Antitermination by GlpP, catabolite repression via CcpA, and inducer exclusion elicited by P-GlpK dephosphorylation control Bacillus subtilis glpFK expression
    • Darbon E, Servant P, Poncet S, Deutscher J. 2002. Antitermination by GlpP, catabolite repression via CcpA, and inducer exclusion elicited by P-GlpK dephosphorylation control Bacillus subtilis glpFK expression. Mol. Microbiol. 43:1039-1052. http://dx.doi.org/10.1046/j.1365-2958 .2002.02800.x.
    • (2002) Mol. Microbiol. , vol.43 , pp. 1039-1052
    • Darbon, E.1    Servant, P.2    Poncet, S.3    Deutscher, J.4
  • 41
    • 0030971645 scopus 로고    scopus 로고
    • Cloning and sequencing of two enterococcal glpK genes and regulation of the encoded glycerol kinases by phosphoenolpyruvate-dependent, phosphotransferase system- catalyzed phosphorylation of a single histidyl residue
    • Charrier V, Buckley E, Parsonage D, Galinier A, Darbon E, Jaquinod M, Forest E, Deutscher J, Claiborne A. 1997. Cloning and sequencing of two enterococcal glpK genes and regulation of the encoded glycerol kinases by phosphoenolpyruvate-dependent, phosphotransferase system- catalyzed phosphorylation of a single histidyl residue. J. Biol. Chem. 272:14166-14174. http://dx.doi.org/10.1074/jbc.272.22.14166.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14166-14174
    • Charrier, V.1    Buckley, E.2    Parsonage, D.3    Galinier, A.4    Darbon, E.5    Jaquinod, M.6    Forest, E.7    Deutscher, J.8    Claiborne, A.9
  • 42
    • 0037446640 scopus 로고    scopus 로고
    • Linkage between fructose 1,6-bisphosphate binding and the dimer-tetramer equilibrium of Escherichia coli glycerol kinase: Critical behavior arising from change of ligand stoichiometry
    • Yu P, Pettigrew DW. 2003. Linkage between fructose 1,6-bisphosphate binding and the dimer-tetramer equilibrium of Escherichia coli glycerol kinase: critical behavior arising from change of ligand stoichiometry. Biochemistry 42:4243-4252. http://dx.doi.org/10.1021/bi027142l.
    • (2003) Biochemistry , vol.42 , pp. 4243-4252
    • Yu, P.1    Pettigrew, D.W.2
  • 44
    • 0027229131 scopus 로고
    • Regulation of glycerol metabolism in Enterococcus faecalis by phosphoenolpyruvate-dependent phosphorylation of glycerol kinase catalyzed by enzyme i and HPr of the phosphotransferase system
    • Deutscher J, Bauer B, Sauerwald H. 1993. Regulation of glycerol metabolism in Enterococcus faecalis by phosphoenolpyruvate-dependent phosphorylation of glycerol kinase catalyzed by enzyme I and HPr of the phosphotransferase system. J. Bacteriol. 175:3730-3733.
    • (1993) J. Bacteriol. , vol.175 , pp. 3730-3733
    • Deutscher, J.1    Bauer, B.2    Sauerwald, H.3
  • 45
    • 0021278017 scopus 로고
    • Regulation of glycerol uptake by the phosphoenolpyruvate-sugar phosphotransferase system in Bacillus subtilis
    • Reizer J, Novotny MJ, Stuiver I, Saier MH, Jr. 1984. Regulation of glycerol uptake by the phosphoenolpyruvate-sugar phosphotransferase system in Bacillus subtilis. J. Bacteriol. 159:243-250.
    • (1984) J. Bacteriol. , vol.159 , pp. 243-250
    • Reizer, J.1    Novotny, M.J.2    Stuiver, I.3    Saier Jr., M.H.4
  • 46
    • 0029065058 scopus 로고
    • Mutations in the glycerol kinase gene restore the ability of a ptsGHI mutant of Bacillus subtilis to grow on glycerol
    • Wehtje C, Beijer L, Nilsson R-P, Rutberg B. 1995. Mutations in the glycerol kinase gene restore the ability of a ptsGHI mutant of Bacillus subtilis to grow on glycerol. Microbiology 141:1193-1198. http://dx.doi .org/10.1099/13500872-141-5-1193.
    • (1995) Microbiology , vol.141 , pp. 1193-1198
    • Wehtje, C.1    Beijer, L.2    Nilsson, R.-P.3    Rutberg, B.4
  • 47
    • 59849123384 scopus 로고    scopus 로고
    • Structural characterizations of glycerol kinase: Unraveling phosphorylation-induced long-range activation
    • Yeh JI, Kettering R, Saxl R, Bourand A, Darbon E, Joly N, Briozzo P, Deutscher J. 2009. Structural characterizations of glycerol kinase: unraveling phosphorylation-induced long-range activation. Biochemistry 48:346-356. http://dx.doi.org/10.1021/bi8009407.
    • (2009) Biochemistry , vol.48 , pp. 346-356
    • Yeh, J.I.1    Kettering, R.2    Saxl, R.3    Bourand, A.4    Darbon, E.5    Joly, N.6    Briozzo, P.7    Deutscher, J.8
  • 48
    • 0024572660 scopus 로고
    • Lactose transport system of Streptococcus thermophilus: A hybrid protein with homology to the melibiose carrier and Enzyme III of phosphoenolpyruvatedependent phosphotransferase systems
    • Poolman B, Royer TJ, Mainzer SE, Schmidt BF. 1989. Lactose transport system of Streptococcus thermophilus: a hybrid protein with homology to the melibiose carrier and Enzyme III of phosphoenolpyruvatedependent phosphotransferase systems. J. Bacteriol. 171:244-253.
    • (1989) J. Bacteriol. , vol.171 , pp. 244-253
    • Poolman, B.1    Royer, T.J.2    Mainzer, S.E.3    Schmidt, B.F.4
  • 50
    • 3042735826 scopus 로고    scopus 로고
    • The Lactobacillus casei ptsHI47T mutation causes overexpression of a LevR-regulated but RpoN-independent operon encoding a mannose class phosphotransferase system
    • Mazé A, Boël G, Poncet S, Mijakovic I, Le Breton Y, Benachour A, Monedero V, Deutscher J, Hartke A. 2004. The Lactobacillus casei ptsHI47T mutation causes overexpression of a LevR-regulated but RpoN-independent operon encoding a mannose class phosphotransferase system. J. Bacteriol. 186:4543-4555. http://dx.doi.org/10.1128/JB .186.14.4543-4555.2004.
    • (2004) J. Bacteriol. , vol.186 , pp. 4543-4555
    • Mazé, A.1    Boël, G.2    Poncet, S.3    Mijakovic, I.4    Le Breton, Y.5    Benachour, A.6    Monedero, V.7    Deutscher, J.8    Hartke, A.9
  • 52
    • 0032927643 scopus 로고    scopus 로고
    • A hybrid response regulator possessing a PEP-dependent phosphorylation domain
    • Reizer J, Schneider B, Reizer A, Saier MH, Jr. 1999. A hybrid response regulator possessing a PEP-dependent phosphorylation domain. Microbiology 145:987-989. http://dx.doi.org/10.1099/13500872-145-5-987.
    • (1999) Microbiology , vol.145 , pp. 987-989
    • Reizer, J.1    Schneider, B.2    Reizer, A.3    Saier Jr., M.H.4
  • 54
    • 15444365483 scopus 로고    scopus 로고
    • The doubly phosphorylated form of HPr, HPr(Ser-P)(His-P), is abundant in exponentially growing cells of Streptococcus thermophilus and phosphorylates the lactose transporter LacS as efficiently as HPr(His-P)
    • Cochu A, Roy D, Vaillancourt K, Lemay JD, Casabon I, Frenette M, Moineau S, Vadeboncoeur C. 2005. The doubly phosphorylated form of HPr, HPr(Ser-P)(His-P), is abundant in exponentially growing cells of Streptococcus thermophilus and phosphorylates the lactose transporter LacS as efficiently as HPr(His-P). Appl. Environ. Microbiol. 71:1364-1372. http://dx.doi.org/10.1128/ AEM.71.3.1364-1372.2005.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 1364-1372
    • Cochu, A.1    Roy, D.2    Vaillancourt, K.3    Lemay, J.D.4    Casabon, I.5    Frenette, M.6    Moineau, S.7    Vadeboncoeur, C.8
  • 55
    • 67649388225 scopus 로고    scopus 로고
    • A metabolic operon in extraintestinal pathogenic Escherichia coli promotes fitness under stressful conditions and invasion of eukaryotic cells
    • Rouquet G, Porcheron G, Barra C, Répérant M, Chanteloup NK, Schouler C, Gilot P. 2009. A metabolic operon in extraintestinal pathogenic Escherichia coli promotes fitness under stressful conditions and invasion of eukaryotic cells. J. Bacteriol. 191:4427-4440. http://dx.doi .org/10.1128/JB.00103-09.
    • (2009) J. Bacteriol. , vol.191 , pp. 4427-4440
    • Rouquet, G.1    Porcheron, G.2    Barra, C.3    Répérant, M.4    Chanteloup, N.K.5    Schouler, C.6    Gilot, P.7
  • 56
    • 0344564161 scopus 로고    scopus 로고
    • Regulation of the lic operon of Bacillus subtilis and characterization of potential phosphorylation sites of the LicR regulator protein by site-directed mutagenesis
    • Tobisch S, Stülke J, Hecker M. 1999. Regulation of the lic operon of Bacillus subtilis and characterization of potential phosphorylation sites of the LicR regulator protein by site-directed mutagenesis. J. Bacteriol. 181: 4995-5003.
    • (1999) J. Bacteriol. , vol.181 , pp. 4995-5003
    • Tobisch, S.1    Stülke, J.2    Hecker, M.3
  • 57
    • 0031943540 scopus 로고    scopus 로고
    • Antagonistic effects of dual PTS-catalysed phosphorylation on the Bacillus subtilis transcriptional activator LevR
    • Martin-Verstraete I, Charrier V, Stülke J, Galinier A, Erni B, Rapoport G, Deutscher J. 1998. Antagonistic effects of dual PTS-catalysed phosphorylation on the Bacillus subtilis transcriptional activator LevR. Mol. Microbiol. 28:293-303. http://dx.doi.org/10.1046/j.1365-2958.1998.00781.x.
    • (1998) Mol. Microbiol. , vol.28 , pp. 293-303
    • Martin-Verstraete, I.1    Charrier, V.2    Stülke, J.3    Galinier, A.4    Erni, B.5    Rapoport, G.6    Deutscher, J.7
  • 58
    • 77952809662 scopus 로고    scopus 로고
    • Control of Bacillus subtilis mtl operon expression by complex phosphorylation-dependent regulation of the transcriptional activator MtlR
    • Joyet P, Derkaoui M, Poncet S, Deutscher J. 2010. Control of Bacillus subtilis mtl operon expression by complex phosphorylation-dependent regulation of the transcriptional activator MtlR. Mol. Microbiol. 76: 1279-1294. http://dx.doi.org/10.1111/j.1365-2958.2010.07175.x.
    • (2010) Mol. Microbiol. , vol.76 , pp. 1279-1294
    • Joyet, P.1    Derkaoui, M.2    Poncet, S.3    Deutscher, J.4
  • 59
    • 0033584860 scopus 로고    scopus 로고
    • Substrate recognition at the cytoplasmic and extracellular binding site of the lactose transport protein of Streptococcus thermophilus
    • Veenhoff LM, Poolman B. 1999. Substrate recognition at the cytoplasmic and extracellular binding site of the lactose transport protein of Streptococcus thermophilus. J. Biol. Chem. 274:33244-33250. http://dx .doi.org/10.1074/jbc. 274.47.33244.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33244-33250
    • Veenhoff, L.M.1    Poolman, B.2
  • 60
    • 0032900617 scopus 로고    scopus 로고
    • Phosphorylation and functional properties of the IIA domain of the lactose transport protein of Streptococcus thermophilus
    • Gunnewijk MGW, Postma PW, Poolman B. 1999. Phosphorylation and functional properties of the IIA domain of the lactose transport protein of Streptococcus thermophilus. J. Bacteriol. 181:632-641.
    • (1999) J. Bacteriol. , vol.181 , pp. 632-641
    • Gunnewijk, M.G.W.1    Postma, P.W.2    Poolman, B.3
  • 61
    • 0345687936 scopus 로고    scopus 로고
    • Phosphorylation of Streptococcus salivarius lactose permease (LacS) by HPr(His-P) and HPr(Ser- P)(His-P) and effects on growth
    • Lessard C, Cochu A, Lemay JD, Roy D, Vaillancourt K, Frenette M, Moineau S, Vadeboncoeur C. 2003. Phosphorylation of Streptococcus salivarius lactose permease (LacS) by HPr(His-P) and HPr(Ser- P)(His-P) and effects on growth. J. Bacteriol. 185:6764-6772. http://dx .doi.org/10.1128/JB.185.23.6764-6772.2003.
    • (2003) J. Bacteriol. , vol.185 , pp. 6764-6772
    • Lessard, C.1    Cochu, A.2    Lemay, J.D.3    Roy, D.4    Vaillancourt, K.5    Frenette, M.6    Moineau, S.7    Vadeboncoeur, C.8
  • 62
    • 0034601988 scopus 로고    scopus 로고
    • HPr(His-P)-mediated phosphorylation differently affects counterflow and proton motive forcedriven uptake via the lactose transport protein of Streptococcus thermophilus
    • Gunnewijk MGW, Poolman B. 2000. HPr(His-P)-mediated phosphorylation differently affects counterflow and proton motive forcedriven uptake via the lactose transport protein of Streptococcus thermophilus. J. Biol. Chem. 275:34080-34085. http://dx.doi.org/10.1074/jbc .M003513200.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34080-34085
    • Gunnewijk, M.G.W.1    Poolman, B.2
  • 63
    • 28544438677 scopus 로고    scopus 로고
    • The activity of the lactose transporter from Streptococcus thermophilus is increased by phosphorylated IIA and the action of beta-galactosidase
    • Geertsma ER, Duurkens RH, Poolman B. 2005. The activity of the lactose transporter from Streptococcus thermophilus is increased by phosphorylated IIA and the action of beta-galactosidase. Biochemistry 44: 15889-15897. http://dx.doi.org/10.1021/bi051638w.
    • (2005) Biochemistry , vol.44 , pp. 15889-15897
    • Geertsma, E.R.1    Duurkens, R.H.2    Poolman, B.3
  • 64
    • 84866409908 scopus 로고    scopus 로고
    • Novel listerial glycerol dehydrogenase- and phosphoenolpyruvatedependent dihydroxyacetone kinase system connected to the pentose phosphate pathway
    • Monniot C, Zébré AC, Aké FMD, Deutscher J, Milohanic E. 2012. Novel listerial glycerol dehydrogenase- and phosphoenolpyruvatedependent dihydroxyacetone kinase system connected to the pentose phosphate pathway. J. Bacteriol. 194:4972-4982. http://dx.doi.org/10 .1128/JB.00801-12.
    • (2012) J. Bacteriol. , vol.194 , pp. 4972-4982
    • Monniot, C.1    Zébré, A.C.2    Aké, F.M.D.3    Deutscher, J.4    Milohanic, E.5
  • 65
    • 84867114728 scopus 로고    scopus 로고
    • Aerobic glycerol dissimilation via the Enterococcus faecalis DhaK pathway depends on NADH oxidase and a phosphotransfer reaction from PEP to DhaK via EIIADha
    • Sauvageot N, Ladjouzi R, Benachour A, Rincé A, Deutscher J, Hartke A. 2012. Aerobic glycerol dissimilation via the Enterococcus faecalis DhaK pathway depends on NADH oxidase and a phosphotransfer reaction from PEP to DhaK via EIIADha. Microbiology 158:2661-2666. http://dx .doi.org/10.1099/mic.0. 061663-0.
    • (2012) Microbiology , vol.158 , pp. 2661-2666
    • Sauvageot, N.1    Ladjouzi, R.2    Benachour, A.3    Rincé, A.4    Deutscher, J.5    Hartke, A.6
  • 66
    • 0032913240 scopus 로고    scopus 로고
    • Role of BkdR, a transcriptional activator of the SigL-dependent isoleucine and valine degradation pathway in Bacillus subtilis
    • Débarbouillé M, Gardan R, Arnaud M, Rapoport G. 1999. Role of BkdR, a transcriptional activator of the SigL-dependent isoleucine and valine degradation pathway in Bacillus subtilis. J. Bacteriol. 181:2059-2066.
    • (1999) J. Bacteriol. , vol.181 , pp. 2059-2066
    • Débarbouillé, M.1    Gardan, R.2    Arnaud, M.3    Rapoport, G.4
  • 67
    • 84890484511 scopus 로고    scopus 로고
    • Nitrogen assimilation in Escherichia coli: Putting molecular data into a systems perspective
    • van Heeswijk WC, Westerhoff HV, Boogerd FC. 2013. Nitrogen assimilation in Escherichia coli: putting molecular data into a systems perspective. Microbiol. Mol. Biol. Rev. 77:628-695. http://dx.doi.org/10 .1128/MMBR.00025-13.
    • (2013) Microbiol. Mol. Biol. Rev. , vol.77 , pp. 628-695
    • Van Heeswijk, W.C.1    Westerhoff, H.V.2    Boogerd, F.C.3
  • 68
    • 84891143422 scopus 로고    scopus 로고
    • Crystal structure of an HD-GYP domain cyclic-di-GMP phosphodiesterase reveals an enzyme with a novel trinuclear catalytic iron centre
    • Bellini D, Caly DL, McCarthy Y, Bumann M, An S-Q, Dow JM, Walsh RPRMA. 2014. Crystal structure of an HD-GYP domain cyclic-di-GMP phosphodiesterase reveals an enzyme with a novel trinuclear catalytic iron centre. Mol. Microbiol. 91:26-38. http://dx.doi.org/10.1111/mmi .12447.
    • (2014) Mol. Microbiol. , vol.91 , pp. 26-38
    • Bellini, D.1    Caly, D.L.2    McCarthy, Y.3    Bumann, M.4    An, S.-Q.5    Dow, J.M.6    Walsh, R.P.R.M.A.7
  • 69
    • 17644378441 scopus 로고    scopus 로고
    • Activation of the LicT transcriptional antiterminator involves a domain swing/lock mechanism provoking massive structural changes
    • Graille M, Zhou CZ, Receveur-Brechot V, Collinet B, Declerck N, van Tilbeurgh H. 2005. Activation of the LicT transcriptional antiterminator involves a domain swing/lock mechanism provoking massive structural changes. J. Biol. Chem. 280:14780-14789. http://dx.doi.org/10.1074/jbc .M414642200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 14780-14789
    • Graille, M.1    Zhou, C.Z.2    Receveur-Brechot, V.3    Collinet, B.4    Declerck, N.5    Van Tilbeurgh, H.6
  • 70
    • 0035898533 scopus 로고    scopus 로고
    • Crystal structure of an activated form of the PTS regulation domain from the LicT transcriptional antiterminator
    • van Tilbeurgh H, Le Coq D, Declerck N. 2001. Crystal structure of an activated form of the PTS regulation domain from the LicT transcriptional antiterminator. EMBO J. 20:3789-3799. http://dx.doi.org/10 .1093/emboj/20.14. 3789.
    • (2001) EMBO J. , vol.20 , pp. 3789-3799
    • Van Tilbeurgh, H.1    Le Coq, D.2    Declerck, N.3
  • 72
    • 0025968911 scopus 로고
    • The transcriptional regulator LevR of Bacillus subtilis has domains homologous to both -54- and phosphotransferase system-dependent regulators
    • Débarbouillé M, Martin-Verstraete I, Klier A, Rapoport G. 1991. The transcriptional regulator LevR of Bacillus subtilis has domains homologous to both -54- and phosphotransferase system-dependent regulators. Proc. Natl. Acad. Sci. U. S. A. 88:2212-2216. http://dx.doi.org/10.1073 /pnas.88.6.2212.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 2212-2216
    • Débarbouillé, M.1    Martin-Verstraete, I.2    Klier, A.3    Rapoport, G.4
  • 73
    • 0032905438 scopus 로고    scopus 로고
    • Regulation of the activity of the Bacillus subtilis antiterminator LicT by multiple PEPdependent, enzyme I- and HPr-catalysed phosphorylation
    • Lindner C, Galinier A, Hecker M, Deutscher J. 1999. Regulation of the activity of the Bacillus subtilis antiterminator LicT by multiple PEPdependent, enzyme I- and HPr-catalysed phosphorylation. Mol. Microbiol. 31:995-1006. http://dx.doi.org/10.1046/j.1365-2958.1999.01262.x.
    • (1999) Mol. Microbiol. , vol.31 , pp. 995-1006
    • Lindner, C.1    Galinier, A.2    Hecker, M.3    Deutscher, J.4
  • 74
    • 0036716732 scopus 로고    scopus 로고
    • Bacillus subtilis mutant LicT antiterminators exhibiting enzyme I- and HPr-independent antitermination affect catabolite repression of the bglPH operon
    • Lindner C, Hecker M, Le Coq D, Deutscher J. 2002. Bacillus subtilis mutant LicT antiterminators exhibiting enzyme I- and HPr-independent antitermination affect catabolite repression of the bglPH operon. J. Bacteriol. 184:4819-4828. http://dx.doi.org/10.1128/JB.184.17.4819-4828 .2002.
    • (2002) J. Bacteriol. , vol.184 , pp. 4819-4828
    • Lindner, C.1    Hecker, M.2    Le Coq, D.3    Deutscher, J.4
  • 75
    • 0034786619 scopus 로고    scopus 로고
    • Sites of positive and negative regulation in the Bacillus subtilis antiterminators LicT and SacY
    • Tortosa P, Declerck N, Dutartre H, Lindner C, Deutscher J, Le Coq D. 2001. Sites of positive and negative regulation in the Bacillus subtilis antiterminators LicT and SacY. Mol. Microbiol. 41:1381-1393. http://dx .doi.org/10.1046/j.1365-2958.2001.02608.x.
    • (2001) Mol. Microbiol. , vol.41 , pp. 1381-1393
    • Tortosa, P.1    Declerck, N.2    Dutartre, H.3    Lindner, C.4    Deutscher, J.5    Le Coq, D.6
  • 76
    • 84891589951 scopus 로고    scopus 로고
    • Regulation of the Bacillus subtilis mannitol utilization genes: Promoter structure and transcriptional activation by the wild-type regulator (MtlR) and its mutants
    • Heravi KM, Altenbuchner J. 2014. Regulation of the Bacillus subtilis mannitol utilization genes: promoter structure and transcriptional activation by the wild-type regulator (MtlR) and its mutants. Microbiology 160:91-101. http://dx.doi.org/10.1099/mic.0.071233-0.
    • (2014) Microbiology , vol.160 , pp. 91-101
    • Heravi, K.M.1    Altenbuchner, J.2
  • 77
    • 34548515942 scopus 로고    scopus 로고
    • Regulation of the mpt operon in Listeria innocua by the ManR protein
    • Xue J, Miller KW. 2007. Regulation of the mpt operon in Listeria innocua by the ManR protein. Appl. Environ. Microbiol. 73:5648-5652. http://dx.doi.org/10.1128/AEM.00052-07.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 5648-5652
    • Xue, J.1    Miller, K.W.2
  • 78
    • 80955178826 scopus 로고    scopus 로고
    • Mutational analysis of glucose transport regulation and glucose-mediated virulence gene repression in Listeria monocytogenes
    • Aké FM, Joyet P, Deutscher J, Milohanic E. 2011. Mutational analysis of glucose transport regulation and glucose-mediated virulence gene repression in Listeria monocytogenes. Mol. Microbiol. 81:274-293. http: //dx.doi.org/10.1111/j.1365-2958.2011.07692.x.
    • (2011) Mol. Microbiol. , vol.81 , pp. 274-293
    • Aké, F.M.1    Joyet, P.2    Deutscher, J.3    Milohanic, E.4
  • 79
    • 69449090624 scopus 로고    scopus 로고
    • Modulation of transcription antitermination in the bgl operon of Escherichia coli by the PTS
    • Raveh H, Lopian L, Nussbaum-Shochat A, Wright A, Amster-Choder O. 2009. Modulation of transcription antitermination in the bgl operon of Escherichia coli by the PTS. Proc. Natl. Acad. Sci. U. S. A. 106:13523-13528. http://dx.doi.org/10.1073/pnas.0902559106.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 13523-13528
    • Raveh, H.1    Lopian, L.2    Nussbaum-Shochat, A.3    Wright, A.4    Amster-Choder, O.5
  • 80
    • 84866859264 scopus 로고    scopus 로고
    • Activation of Escherichia coli antiterminator BglG requires its phosphorylation
    • Rothe FM, Bahr T, Stülke J, Rak B, Görke B. 2012. Activation of Escherichia coli antiterminator BglG requires its phosphorylation. Proc. Natl. Acad. Sci. U. S. A. 109:15906-15911. http://dx.doi.org/10.1073 /pnas.1210443109.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 15906-15911
    • Rothe, F.M.1    Bahr, T.2    Stülke, J.3    Rak, B.4    Görke, B.5
  • 82
    • 84879014996 scopus 로고    scopus 로고
    • PTS phosphorylation of Mga modulates regulon expression and viru- lence in the group A streptococcus
    • Hondorp ER, Hou SC, Hause LL, Gera K, Lee CE, McIver KS. 2013. PTS phosphorylation of Mga modulates regulon expression and viru- lence in the group A streptococcus. Mol. Microbiol. 88:1176-1193. http: //dx.doi.org/10.1111/mmi. 12250.
    • (2013) Mol. Microbiol. , vol.88 , pp. 1176-1193
    • Hondorp, E.R.1    Hou, S.C.2    Hause, L.L.3    Gera, K.4    Lee, C.E.5    McIver, K.S.6
  • 83
    • 33846239261 scopus 로고    scopus 로고
    • Opposing effects of histidine phosphorylation regulate the AtxA virulence transcription factor in Bacillus anthracis
    • Tsvetanova B, Wilson AC, Bongiorni C, Chiang C, Hoch JA, Perego M. 2007. Opposing effects of histidine phosphorylation regulate the AtxA virulence transcription factor in Bacillus anthracis. Mol. Microbiol. 63:644-655. http://dx.doi.org/10.1111/j.1365-2958.2006.05543.x.
    • (2007) Mol. Microbiol. , vol.63 , pp. 644-655
    • Tsvetanova, B.1    Wilson, A.C.2    Bongiorni, C.3    Chiang, C.4    Hoch, J.A.5    Perego, M.6
  • 84
    • 36148948693 scopus 로고    scopus 로고
    • The catabolite control protein CcpA binds to Pmga and influences expression of the virulence regulator Mga in the group A streptococcus
    • Almengor AC, Kinkel TL, Day SJ, McIver KS. 2007. The catabolite control protein CcpA binds to Pmga and influences expression of the virulence regulator Mga in the group A streptococcus. J. Bacteriol. 189: 8405-8416. http://dx.doi.org/10.1128/JB.01038-07.
    • (2007) J. Bacteriol. , vol.189 , pp. 8405-8416
    • Almengor, A.C.1    Kinkel, T.L.2    Day, S.J.3    McIver, K.S.4
  • 88
    • 0021288128 scopus 로고
    • Interaction between IIIGlc of the phosphoenolpyruvate:sugar phosphotransferase system and glycerol kinase of Salmonella typhimurium
    • Postma PW, Epstein W, Schuitema ARJ, Nelson SO. 1984. Interaction between IIIGlc of the phosphoenolpyruvate:sugar phosphotransferase system and glycerol kinase of Salmonella typhimurium. J. Bacteriol. 158: 351-353.
    • (1984) J. Bacteriol. , vol.158 , pp. 351-353
    • Postma, P.W.1    Epstein, W.2    Schuitema, A.R.J.3    Nelson, S.O.4
  • 90
    • 0025904264 scopus 로고
    • The activities of the Escherichia coli MalK protein in maltose transport, regulation, and inducer exclusion can be separated by mutations
    • Kühnau S, Reyes M, Sievertsen A, Shuman HA, Boos W. 1991. The activities of the Escherichia coli MalK protein in maltose transport, regulation, and inducer exclusion can be separated by mutations. J. Bacteriol. 173:2180-2186.
    • (1991) J. Bacteriol. , vol.173 , pp. 2180-2186
    • Kühnau, S.1    Reyes, M.2    Sievertsen, A.3    Shuman, H.A.4    Boos, W.5
  • 91
    • 0019983630 scopus 로고
    • Regulation of lactose permease activity by the phosphoenolpyruvate:sugar phosphotransferase system: Evidence for direct binding of the glucose-specific enzyme III to the lactose permease
    • Osumi T, Saier MH, Jr. 1982. Regulation of lactose permease activity by the phosphoenolpyruvate:sugar phosphotransferase system: evidence for direct binding of the glucose-specific enzyme III to the lactose permease. Proc. Natl. Acad. Sci. U. S. A. 79:1457-1461. http://dx.doi.org/10 .1073/pnas.79.5.1457.
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 1457-1461
    • Osumi, T.1    Saier Jr., M.H.2
  • 92
    • 0037197258 scopus 로고    scopus 로고
    • Binding of enzyme IIAGlc, a component of the phosphoenolpyruvate:sugar phosphotransferase system, to the Escherichia coli lactose permease
    • Sondej M, Weinglass AB, Peterkofsky A, Kaback HR. 2002. Binding of enzyme IIAGlc, a component of the phosphoenolpyruvate:sugar phosphotransferase system, to the Escherichia coli lactose permease. Biochemistry 41:5556-5565. http://dx.doi.org/10.1021/bi011990j.
    • (2002) Biochemistry , vol.41 , pp. 5556-5565
    • Sondej, M.1    Weinglass, A.B.2    Peterkofsky, A.3    Kaback, H.R.4
  • 93
    • 0021030406 scopus 로고
    • Cooperative binding of the sugar substrates and allosteric regulatory protein (enzyme IIIGlc of the phosphotransferase system) to the lactose and melibiose permeases in Escherichia coli and Salmonella typhimurium
    • Saier MH, Jr, Novotny MJ, Comeau-Fuhrman D, Osumi T, Desai JD. 1983. Cooperative binding of the sugar substrates and allosteric regulatory protein (enzyme IIIGlc of the phosphotransferase system) to the lactose and melibiose permeases in Escherichia coli and Salmonella typhimurium. J. Bacteriol. 155:1351-1357.
    • (1983) J. Bacteriol. , vol.155 , pp. 1351-1357
    • Saier Jr., M.H.1    Novotny, M.J.2    Comeau-Fuhrman, D.3    Osumi, T.4    Desai, J.D.5
  • 94
    • 0022531321 scopus 로고
    • Regulation of glycerol kinase by enzyme IIIGlc of the phosphoenolpyruvate:carbohydrate phosphotransferase system
    • de Boer M, Broekhuizen CP, Postma PW. 1986. Regulation of glycerol kinase by enzyme IIIGlc of the phosphoenolpyruvate:carbohydrate phosphotransferase system. J. Bacteriol. 167:393-395.
    • (1986) J. Bacteriol. , vol.167 , pp. 393-395
    • De Boer, M.1    Broekhuizen, C.P.2    Postma, P.W.3
  • 95
    • 34547761711 scopus 로고    scopus 로고
    • Replacing the general energy-coupling proteins of the phospho-enolpyruvate: Sugar phosphotransferase system of Salmonella typhimurium with fructose-inducible counterparts results in the inability to utilize nonphosphotransferase system sugars
    • Sutrina SL, Inniss PI, Lazarus LA, Inglis L, Maximilien J. 2007. Replacing the general energy-coupling proteins of the phospho-enolpyruvate: sugar phosphotransferase system of Salmonella typhimurium with fructose-inducible counterparts results in the inability to utilize nonphosphotransferase system sugars. Can. J. Microbiol. 53:586-598. http://dx.doi.org/10.1139/W07-020.
    • (2007) Can. J. Microbiol. , vol.53 , pp. 586-598
    • Sutrina, S.L.1    Inniss, P.I.2    Lazarus, L.A.3    Inglis, L.4    Maximilien, J.5
  • 96
    • 0026754433 scopus 로고
    • Resistance of the melibiose carrier to inhibition by the phosphotransferase system due to substitutions of amino acid residues in the carrier of Salmonella typhimurium
    • Kuroda M, De Waard S, Mizushima K, Tsuda M, Postma P, Tsuchiya T. 1992. Resistance of the melibiose carrier to inhibition by the phosphotransferase system due to substitutions of amino acid residues in the carrier of Salmonella typhimurium. J. Biol. Chem. 267:18336-18341.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18336-18341
    • Kuroda, M.1    De Waard, S.2    Mizushima, K.3    Tsuda, M.4    Postma, P.5    Tsuchiya, T.6
  • 97
    • 0027972706 scopus 로고
    • Regulation of the raffinose permease of Escherichia coli by the glucose-specific enzyme IIA of the phosphoenolpyruvate:sugar phosphotransferase system
    • Titgemeyer F, Mason RE, Saier MH, Jr. 1994. Regulation of the raffinose permease of Escherichia coli by the glucose-specific enzyme IIA of the phosphoenolpyruvate:sugar phosphotransferase system. J. Bacteriol. 176:543-546.
    • (1994) J. Bacteriol. , vol.176 , pp. 543-546
    • Titgemeyer, F.1    Mason, R.E.2    Saier Jr., M.H.3
  • 99
    • 0029816938 scopus 로고    scopus 로고
    • Involvement of the central loop of the lactose permease of Escherichia coli in its allosteric regulation by the glucose-specific enzyme IIA of the phosphoenolpyruvate- dependent phosphotransferase system
    • Hoischen C, Levin J, Pitaknarongphorn S, Reizer J, Saier MH, Jr. 1996. Involvement of the central loop of the lactose permease of Escherichia coli in its allosteric regulation by the glucose-specific enzyme IIA of the phosphoenolpyruvate- dependent phosphotransferase system. J. Bacteriol. 178:6082-6086.
    • (1996) J. Bacteriol. , vol.178 , pp. 6082-6086
    • Hoischen, C.1    Levin, J.2    Pitaknarongphorn, S.3    Reizer, J.4    Saier Jr., M.H.5
  • 100
    • 0030089476 scopus 로고    scopus 로고
    • Mechanism responsible for glucoselactose diauxie in Escherichia coli: Challenge to the cAMP model
    • Inada T, Kimata K, Aiba H. 1996. Mechanism responsible for glucoselactose diauxie in Escherichia coli: challenge to the cAMP model. Genes Cells 1:293-301. http://dx.doi.org/10.1046/j.1365-2443.1996.24025.x.
    • (1996) Genes Cells , vol.1 , pp. 293-301
    • Inada, T.1    Kimata, K.2    Aiba, H.3
  • 101
    • 78249244785 scopus 로고    scopus 로고
    • A mammalian insulysin homolog is regulated by enzyme IIAGlc of the glucose transport system in Vibrio vulnificus
    • Kim YJ, Ryu Y, Koo BM, Lee NY, Chun SJ, Park SJ, Lee KH, Seok YJ. 2010. A mammalian insulysin homolog is regulated by enzyme IIAGlc of the glucose transport system in Vibrio vulnificus. FEBS Lett. 584:4537-4544. http://dx.doi.org/10.1016/j.febslet.2010.10.035.
    • (2010) FEBS Lett. , vol.584 , pp. 4537-4544
    • Kim, Y.J.1    Ryu, Y.2    Koo, B.M.3    Lee, N.Y.4    Chun, S.J.5    Park, S.J.6    Lee, K.H.7    Seok, Y.J.8
  • 102
    • 84872139665 scopus 로고    scopus 로고
    • Glucose-specific enzyme IIA has unique binding partners in the Vibrio cholerae biofilm
    • Pickering BS, Smith DR, Watnick PI. 2012. Glucose-specific enzyme IIA has unique binding partners in the Vibrio cholerae biofilm. mBio 3(6):e00228-12. http://dx.doi.org/10.1128/mBio.00228-12.
    • (2012) MBio , vol.3 , Issue.6
    • Pickering, B.S.1    Smith, D.R.2    Watnick, P.I.3
  • 103
    • 33748705968 scopus 로고    scopus 로고
    • Identification of a novel regulatory protein (CsrD) that targets the global regulatory RNAs CsrB and CsrC for degradation by RNase e
    • Suzuki K, Babitzke P, Kushner SR, Romeo T. 2006. Identification of a novel regulatory protein (CsrD) that targets the global regulatory RNAs CsrB and CsrC for degradation by RNase E. Genes Dev. 20:2605-2617. http://dx.doi.org/10. 1101/gad.1461606.
    • (2006) Genes Dev. , vol.20 , pp. 2605-2617
    • Suzuki, K.1    Babitzke, P.2    Kushner, S.R.3    Romeo, T.4
  • 104
    • 3843067740 scopus 로고    scopus 로고
    • A novel fermentation/respiration switch protein regulated by enzyme IIAGlc in Escherichia coli
    • Koo BM, Yoon MJ, Lee CR, Nam TW, Choe YJ, Jaffe H, Peterkofsky A, Seok YJ. 2004. A novel fermentation/respiration switch protein regulated by enzyme IIAGlc in Escherichia coli. J. Biol. Chem. 279:31613-31621. http://dx.doi.org/ 10.1074/jbc.M405048200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31613-31621
    • Koo, B.M.1    Yoon, M.J.2    Lee, C.R.3    Nam, T.W.4    Choe, Y.J.5    Jaffe, H.6    Peterkofsky, A.7    Seok, Y.J.8
  • 105
    • 0032492662 scopus 로고    scopus 로고
    • Cation promoted association of Escherichia coli phosphocarrier protein IIAGlc with regulatory target protein glycerol kinase: Substitutions of a Zn(II) ligand and implications for inducer exclusion
    • Pettigrew DW, Meadow ND, Roseman S, Remington SJ. 1998. Cation promoted association of Escherichia coli phosphocarrier protein IIAGlc with regulatory target protein glycerol kinase: substitutions of a Zn(II) ligand and implications for inducer exclusion. Biochemistry 37:4875-4883. http://dx.doi.org/10.1021/bi971634u.
    • (1998) Biochemistry , vol.37 , pp. 4875-4883
    • Pettigrew, D.W.1    Meadow, N.D.2    Roseman, S.3    Remington, S.J.4
  • 106
    • 84880511070 scopus 로고    scopus 로고
    • Carbon catabolite repression of the maltose transporter revealed by X-ray crystallography
    • Chen S, Oldham ML, Davidson AL, Chen J. 2013. Carbon catabolite repression of the maltose transporter revealed by X-ray crystallography. Nature 499:364-368. http://dx.doi.org/10.1038/nature12232.
    • (2013) Nature , vol.499 , pp. 364-368
    • Chen, S.1    Oldham, M.L.2    Davidson, A.L.3    Chen, J.4
  • 107
    • 0034329415 scopus 로고    scopus 로고
    • Solution structure of the phosphoryl transfer complex between the signal transducing proteins HPr and IIAGlucose of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system
    • Wang GS, Louis JM, Sondej M, Seok Y-J, Peterkofsky A, Clore GM. 2000. Solution structure of the phosphoryl transfer complex between the signal transducing proteins HPr and IIAGlucose of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system. EMBO J. 19: 5635-5649. http://dx.doi.org/10.1093/emboj/19.21.5635.
    • (2000) EMBO J. , vol.19 , pp. 5635-5649
    • Wang, G.S.1    Louis, J.M.2    Sondej, M.3    Seok, Y.-J.4    Peterkofsky, A.5    Clore, G.M.6
  • 108
    • 0042090323 scopus 로고    scopus 로고
    • Solution structure of the phosphoryl transfer complex between the signal transducing protein IIAGlucose and the cytoplasmic domain of the glucose transporter IICBGlucose of the Escherichia coli glucose phosphotransferase system
    • Cai M, Williams DC, Jr, Wang G, Lee BR, Peterkofsky A, Clore GM. 2003. Solution structure of the phosphoryl transfer complex between the signal transducing protein IIAGlucose and the cytoplasmic domain of the glucose transporter IICBGlucose of the Escherichia coli glucose phosphotransferase system. J. Biol. Chem. 278:25191-25206. http://dx.doi.org/10 .1074/jbc.M302677200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25191-25206
    • Cai, M.1    Williams Jr., D.C.2    Wang, G.3    Lee, B.R.4    Peterkofsky, A.5    Clore, G.M.6
  • 112
    • 0000103309 scopus 로고
    • The role of genes downstream of the N structural gene rpoN in Klebsiella pneumonia
    • Tikhonovitch IA, Provorov NA, Romanov VI, Newton WE (ed), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Merrick MJ, Taylor M, Saier MH, Jr, Reizer J. 1995. The role of genes downstream of the N structural gene rpoN in Klebsiella pneumoniae, p 189-194. In Tikhonovitch IA, Provorov NA, Romanov VI, Newton WE (ed), Nitrogen fixation: fundamentals and applications. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1995) Nitrogen Fixation: Fundamentals and Applications , pp. 189-194
    • Merrick, M.J.1    Taylor, M.2    Saier Jr., M.H.3    Reizer, J.4
  • 113
    • 77952552068 scopus 로고    scopus 로고
    • Regulatory roles of the bacterial nitrogen- related phosphotransferase system
    • Pflüger-Grau K, Görke B. 2010. Regulatory roles of the bacterial nitrogen- related phosphotransferase system. Trends Microbiol. 18:205-214. http://dx.doi.org/10.1016/j.tim.2010.02.003.
    • (2010) Trends Microbiol. , vol.18 , pp. 205-214
    • Pflüger-Grau, K.1    Görke, B.2
  • 114
    • 42549106523 scopus 로고    scopus 로고
    • Evidence of in vivo cross talk between the nitrogen-related and fructose-related branches of the carbohydrate phosphotransferase system of Pseudomonas putida
    • Pflüger K, de Lorenzo V. 2008. Evidence of in vivo cross talk between the nitrogen-related and fructose-related branches of the carbohydrate phosphotransferase system of Pseudomonas putida. J. Bacteriol. 190: 3374-3380. http://dx.doi.org/10.1128/JB.02002-07.
    • (2008) J. Bacteriol. , vol.190 , pp. 3374-3380
    • Pflüger, K.1    De Lorenzo, V.2
  • 115
    • 47849122007 scopus 로고    scopus 로고
    • Requirements for the phosphorylation of the Escherichia coli EIIANtr protein in vivo
    • Zimmer B, Hillmann A, Görke B. 2008. Requirements for the phosphorylation of the Escherichia coli EIIANtr protein in vivo. FEMS Microbiol. Lett. 286:96-102. http://dx.doi.org/10.1111/j.1574-6968.2008 .01262.x.
    • (2008) FEMS Microbiol. Lett. , vol.286 , pp. 96-102
    • Zimmer, B.1    Hillmann, A.2    Görke, B.3
  • 116
    • 84876703328 scopus 로고    scopus 로고
    • Reciprocal regulation of the autophosphorylation of enzyme INtr by glutamine and -ketoglutarate in Escherichia coli
    • Lee CR, Park YH, Kim M, Kim YR, Park S, Peterkofsky A, Seok YJ. 2013. Reciprocal regulation of the autophosphorylation of enzyme INtr by glutamine and -ketoglutarate in Escherichia coli. Mol. Microbiol. 88:473-485. http://dx.doi.org/10.1111/mmi.12196.
    • (2013) Mol. Microbiol. , vol.88 , pp. 473-485
    • Lee, C.R.1    Park, Y.H.2    Kim, M.3    Kim, Y.R.4    Park, S.5    Peterkofsky, A.6    Seok, Y.J.7
  • 117
    • 84874881006 scopus 로고    scopus 로고
    • Tar- geted decay of a regulatory small RNA by an adaptor protein for RNase e and counteraction by an anti-adaptor RNA
    • Göpel Y, Papenfort K, Reichenbach B, Vogel J, Görke B. 2013. Tar- geted decay of a regulatory small RNA by an adaptor protein for RNase E and counteraction by an anti-adaptor RNA. Genes Dev. 27:552-564. http://dx.doi.org/10.1101/gad.210112.112.
    • (2013) Genes Dev. , vol.27 , pp. 552-564
    • Göpel, Y.1    Papenfort, K.2    Reichenbach, B.3    Vogel, J.4    Görke, B.5
  • 118
    • 84898839899 scopus 로고    scopus 로고
    • Biochemical characterization of a nitrogen-type phosphotransferase system reveals enzyme EINtr integrates carbon and nitrogen signaling in Sinorhizobium meliloti
    • 14 March
    • Goodwin RA, Gage DJ. 14 March 2014. Biochemical characterization of a nitrogen-type phosphotransferase system reveals enzyme EINtr integrates carbon
    • (2014) J. Bacteriol
    • Goodwin, R.A.1    Gage, D.J.2
  • 121
    • 84876208373 scopus 로고    scopus 로고
    • Gating of the TrkH ion channel by its associated RCK protein TrkA
    • Cao Y, Pan Y, Huang H, Jin X, Levin EJ, Kloss B, Zhou M. 2013. Gating of the TrkH ion channel by its associated RCK protein TrkA. Nature 496:317-322. http://dx.doi.org/10.1038/nature12056.
    • (2013) Nature , vol.496 , pp. 317-322
    • Cao, Y.1    Pan, Y.2    Huang, H.3    Jin, X.4    Levin, E.J.5    Kloss, B.6    Zhou, M.7
  • 122
    • 78650034955 scopus 로고    scopus 로고
    • Potassium mediates Escherichia coli enzyme IIANtr-dependent regulation of sigma factor selectivity
    • Lee CR, Cho SH, Kim HJ, Kim M, Peterkofsky A, Seok YJ. 2010. Potassium mediates Escherichia coli enzyme IIANtr-dependent regulation of sigma factor selectivity. Mol. Microbiol. 78:1468-1483. http://dx.doi .org/10.1111/j.1365- 2958.2010.07419.x.
    • (2010) Mol. Microbiol. , vol.78 , pp. 1468-1483
    • Lee, C.R.1    Cho, S.H.2    Kim, H.J.3    Kim, M.4    Peterkofsky, A.5    Seok, Y.J.6
  • 123
    • 33744502868 scopus 로고    scopus 로고
    • Prokaryotic Kdp-ATPase: Recent insights into the structure and function of KdpB
    • Haupt M, Bramkamp M, Coles M, Kessler H, Altendorf K. 2005. Prokaryotic Kdp-ATPase: recent insights into the structure and function of KdpB. J. Mol. Microbiol. Biotechnol. 10:120-131. http://dx.doi.org /10.1159/000091559.
    • (2005) J. Mol. Microbiol. Biotechnol. , vol.10 , pp. 120-131
    • Haupt, M.1    Bramkamp, M.2    Coles, M.3    Kessler, H.4    Altendorf, K.5
  • 124
    • 84879029281 scopus 로고    scopus 로고
    • The sensor kinase KdpD of Escherichia coli senses external K+
    • Laermann V, Cudic E, Kipschull K, Zimmann P, Altendorf K. 2013. The sensor kinase KdpD of Escherichia coli senses external K+. Mol. Microbiol. 88:1194-1204. http://dx.doi.org/10.1111/mmi.12251.
    • (2013) Mol. Microbiol. , vol.88 , pp. 1194-1204
    • Laermann, V.1    Cudic, E.2    Kipschull, K.3    Zimmann, P.4    Altendorf, K.5
  • 125
    • 0345803937 scopus 로고    scopus 로고
    • The N-terminal input domain of the sensor kinase KdpD of Escherichia coli stabilizes the interaction between the cognate response regulator KdpE and the corresponding DNA-binding site
    • Heermann R, Altendorf K, Jung K. 2003. The N-terminal input domain of the sensor kinase KdpD of Escherichia coli stabilizes the interaction between the cognate response regulator KdpE and the corresponding DNA-binding site. J. Biol. Chem. 278:51277-51284. http://dx.doi.org/10 .1074/jbc.M303801200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 51277-51284
    • Heermann, R.1    Altendorf, K.2    Jung, K.3
  • 126
    • 65549161404 scopus 로고    scopus 로고
    • Stimulation of the potassium sensor KdpD kinase activity by interaction with the phosphotransferase protein IIANtr in Escherichia coli
    • Lüttmann D, Heermann R, Zimmer B, Hillmann A, Rampp IS, Jung K, Görke B. 2009. Stimulation of the potassium sensor KdpD kinase activity by interaction with the phosphotransferase protein IIANtr in Escherichia coli. Mol. Microbiol. 72:978-994. http://dx.doi.org/10.1111 /j.1365-2958.2009.06704.x.
    • (2009) Mol. Microbiol. , vol.72 , pp. 978-994
    • Lüttmann, D.1    Heermann, R.2    Zimmer, B.3    Hillmann, A.4    Rampp, I.S.5    Jung, K.6    Görke, B.7
  • 128
    • 84867058327 scopus 로고    scopus 로고
    • The phosphotransferase protein EIIANtr modulates the phosphate starvation response through interaction with histidine kinase PhoR in Escherichia coli
    • Lüttmann D, Göpel Y, Görke B. 2012. The phosphotransferase protein EIIANtr modulates the phosphate starvation response through interaction with histidine kinase PhoR in Escherichia coli. Mol. Microbiol. 86: 96-110. http://dx.doi.org/10.1111/j.1365-2958.2012.08176.x.
    • (2012) Mol. Microbiol. , vol.86 , pp. 96-110
    • Lüttmann, D.1    Göpel, Y.2    Görke, B.3
  • 129
    • 80052067349 scopus 로고    scopus 로고
    • The interplay of the EIIANtr component of the nitrogen-related phosphotransferase system (PTSNtr) of Pseudomonas putida with pyruvate dehydrogenase
    • Pflüger-Grau K, Chavarría M, de Lorenzo V. 2011. The interplay of the EIIANtr component of the nitrogen-related phosphotransferase system (PTSNtr) of Pseudomonas putida with pyruvate dehydrogenase. Biochim. Biophys. Acta 1810:995-1005. http://dx.doi.org/10.1016/j.bbagen.2011 .01.002.
    • (2011) Biochim. Biophys. Acta , vol.1810 , pp. 995-1005
    • Pflüger-Grau, K.1    Chavarría, M.2    De Lorenzo, V.3
  • 130
    • 67650066590 scopus 로고    scopus 로고
    • Glucose and glycolysis are required for the successful infection of macrophages and mice by Salmonella enterica serovar Typhimurium
    • Bowden SD, Rowley G, Hinton JC, Thompson A. 2009. Glucose and glycolysis are required for the successful infection of macrophages and mice by Salmonella enterica serovar Typhimurium. Infect. Immun. 77: 3117-3126. http://dx.doi.org/ 10.1128/IAI.00093-09.
    • (2009) Infect. Immun. , vol.77 , pp. 3117-3126
    • Bowden, S.D.1    Rowley, G.2    Hinton, J.C.3    Thompson, A.4
  • 131
    • 78650576503 scopus 로고    scopus 로고
    • Salmonella pathogenicity island 2 expression negatively controlled by EIIANtr-SsrB interaction is required for Salmonella virulence
    • Choi J, Shin D, Yoon H, Kim J, Lee CR, Kim M, Seok YJ, Ryu S. 2010. Salmonella pathogenicity island 2 expression negatively controlled by EIIANtr-SsrB interaction is required for Salmonella virulence. Proc. Natl. Acad. Sci. U. S. A. 107:20506-20511. http://dx.doi.org/10.1073/pnas .1000759107.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 20506-20511
    • Choi, J.1    Shin, D.2    Yoon, H.3    Kim, J.4    Lee, C.R.5    Kim, M.6    Seok, Y.J.7    Ryu, S.8
  • 132
    • 26244460328 scopus 로고    scopus 로고
    • Requirement of the dephospho-form of enzyme IIANtr for derepression of Escherichia coli K-12 ilvBN expression
    • Lee CR, Koo BM, Cho SH, Kim YJ, Yoon MJ, Peterkofsky A, Seok YJ. 2005. Requirement of the dephospho-form of enzyme IIANtr for derepression of Escherichia coli K-12 ilvBN expression. Mol. Microbiol. 58: 334-344. http://dx.doi.org/10.1111/j.1365-2958.2005.04834.x.
    • (2005) Mol. Microbiol. , vol.58 , pp. 334-344
    • Lee, C.R.1    Koo, B.M.2    Cho, S.H.3    Kim, Y.J.4    Yoon, M.J.5    Peterkofsky, A.6    Seok, Y.J.7
  • 133
    • 84897052730 scopus 로고    scopus 로고
    • The phosphotransferase protein EIIANtr interacts with SpoT, a key enzyme of the stringent response, in Ralstonia eutropha H16
    • Karstens K, Zschiedrich CP, Bowien B, Stülke J, Görke B. 2014. The phosphotransferase protein EIIANtr interacts with SpoT, a key enzyme of the stringent response, in Ralstonia eutropha H16. Microbiology 160: 711-722. http://dx.doi.org/10.1099/mic.0.075226-0.
    • (2014) Microbiology , vol.160 , pp. 711-722
    • Karstens, K.1    Zschiedrich, C.P.2    Bowien, B.3    Stülke, J.4    Görke, B.5
  • 134
    • 0034675924 scopus 로고    scopus 로고
    • A novel regulatory role of glucose transporter of Escherichia coli: Membrane sequestration of a global repressor Mlc
    • Tanaka Y, Kimata K, Aiba H. 2000. A novel regulatory role of glucose transporter of Escherichia coli: membrane sequestration of a global repressor Mlc. EMBO J. 19:5344-5352. http://dx.doi.org/10.1093/emboj /19.20.5344.
    • (2000) EMBO J. , vol.19 , pp. 5344-5352
    • Tanaka, Y.1    Kimata, K.2    Aiba, H.3
  • 135
    • 0034675992 scopus 로고    scopus 로고
    • Signal transduction between a membrane-bound transporter, PtsG, and a soluble transcription factor, Mlc, of Escherichia coli
    • Lee SJ, Boos W, Bouche JP, Plumbridge J. 2000. Signal transduction between a membrane-bound transporter, PtsG, and a soluble transcription factor, Mlc, of Escherichia coli. EMBO J. 19:5353-5361. http://dx.doi .org/10.1093/emboj/19.20.5353.
    • (2000) EMBO J. , vol.19 , pp. 5353-5361
    • Lee, S.J.1    Boos, W.2    Bouche, J.P.3    Plumbridge, J.4
  • 137
    • 85007744911 scopus 로고
    • Decreasing accumulation of acetate in a rich medium by Escherichia coli on introduction of genes on a multicopy plasmid
    • Hosono K, Kakuda H, Ichihara S. 1995. Decreasing accumulation of acetate in a rich medium by Escherichia coli on introduction of genes on a multicopy plasmid. Biosci. Biotechnol. Biochem. 59:256-261. http: //dx.doi.org/10.1271/ bbb.59.256.
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 256-261
    • Hosono, K.1    Kakuda, H.2    Ichihara, S.3
  • 138
    • 0031973888 scopus 로고    scopus 로고
    • Control of the expression of the manXYZ operon in Escherichia coli: Mlc is a negative regulator of the mannose PTS
    • Plumbridge J. 1998. Control of the expression of the manXYZ operon in Escherichia coli: Mlc is a negative regulator of the mannose PTS. Mol. Microbiol. 27:369-380. http://dx.doi.org/10.1046/j.1365-2958 .1998.00685.x.
    • (1998) Mol. Microbiol. , vol.27 , pp. 369-380
    • Plumbridge, J.1
  • 139
    • 0033877256 scopus 로고    scopus 로고
    • Glucose transporter mutants of Escherichia coli K-12 with changes in substrate recognition of IICBGlc and induction behavior of the ptsG gene
    • Zeppenfeld T, Larisch C, Lengeler JW, Jahreis K. 2000. Glucose transporter mutants of Escherichia coli K-12 with changes in substrate recognition of IICBGlc and induction behavior of the ptsG gene. J. Bacteriol. 182:4443-4452. http://dx.doi.org/10.1128/JB.182.16.4443-4452.2000.
    • (2000) J. Bacteriol. , vol.182 , pp. 4443-4452
    • Zeppenfeld, T.1    Larisch, C.2    Lengeler, J.W.3    Jahreis, K.4
  • 140
    • 0033062699 scopus 로고    scopus 로고
    • Expression of the phosphotransferase system both mediates and is mediated by Mlc regulation in Escherichia coli
    • Plumbridge J. 1999. Expression of the phosphotransferase system both mediates and is mediated by Mlc regulation in Escherichia coli. Mol. Microbiol. 33:260-273. http://dx.doi.org/10.1046/j.1365-2958 .1999.01462.x.
    • (1999) Mol. Microbiol. , vol.33 , pp. 260-273
    • Plumbridge, J.1
  • 141
    • 0037855776 scopus 로고    scopus 로고
    • Analysis of the interaction between the global regulator Mlc and EIIBGlc of the glucose- specific phosphotransferase system in Escherichia coli
    • Seitz S, Lee SJ, Pennetier C, Boos W, Plumbridge J. 2003. Analysis of the interaction between the global regulator Mlc and EIIBGlc of the glucose- specific phosphotransferase system in Escherichia coli. J. Biol. Chem. 278:10744-10751. http://dx.doi.org/10.1074/jbc.M212066200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10744-10751
    • Seitz, S.1    Lee, S.J.2    Pennetier, C.3    Boos, W.4    Plumbridge, J.5
  • 142
    • 41649085020 scopus 로고    scopus 로고
    • Analyses of Mlc-IIBGlc interaction and a plausible molecular mechanism of Mlc inactivation by membrane sequestration
    • Nam TW, Jung HI, An YJ, Park YH, Lee SH, Seok YJ, Cha SS. 2008. Analyses of Mlc-IIBGlc interaction and a plausible molecular mechanism of Mlc inactivation by membrane sequestration. Proc. Natl. Acad. Sci. U. S. A. 105:3751-3756. http://dx.doi.org/10.1073/pnas.0709295105.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 3751-3756
    • Nam, T.W.1    Jung, H.I.2    An, Y.J.3    Park, Y.H.4    Lee, S.H.5    Seok, Y.J.6    Cha, S.S.7
  • 143
    • 3843085214 scopus 로고    scopus 로고
    • Membrane localization itself but not binding to IICB is directly responsible for the inactivation of the global repressor Mlc in Escherichia coli
    • Tanaka Y, Itoh F, Kimata K, Aiba H. 2004. Membrane localization itself but not binding to IICB is directly responsible for the inactivation of the global repressor Mlc in Escherichia coli. Mol. Microbiol. 53:941-951. http://dx.doi.org/10.1111/j.1365-2958.2004.04179.x.
    • (2004) Mol. Microbiol. , vol.53 , pp. 941-951
    • Tanaka, Y.1    Itoh, F.2    Kimata, K.3    Aiba, H.4
  • 144
    • 37349036156 scopus 로고    scopus 로고
    • Different regions of Mlc and NagC, homologous transcriptional repressors controlling expression of the glucose and N-acetylglucosamine phosphotransferase systems in Escherichia coli, are required for inducer signal recognition
    • Pennetier C, Domínguez-Ramírez L, Plumbridge J. 2008. Different regions of Mlc and NagC, homologous transcriptional repressors controlling expression of the glucose and N-acetylglucosamine phosphotransferase systems in Escherichia coli, are required for inducer signal recognition. Mol. Microbiol. 67:364-377. http://dx.doi.org/10.1111/j .1365-2958.2007.06041.x.
    • (2008) Mol. Microbiol. , vol.67 , pp. 364-377
    • Pennetier, C.1    Domínguez-Ramírez, L.2    Plumbridge, J.3
  • 145
    • 84857883145 scopus 로고    scopus 로고
    • Characterization of MtfA, a novel regulatory output signal protein of the glucose-phosphotransferase system in Escherichia coli K-12
    • Göhler AK, Staab A, Gabor E, Homann K, Klang E, Kosfeld A, Muus JE, Wulftange JS, Jahreis K. 2012. Characterization of MtfA, a novel regulatory output signal protein of the glucose-phosphotransferase system in Escherichia coli K-12. J. Bacteriol. 194:1024-1035. http://dx.doi .org/10.1128/JB.06387-11.
    • (2012) J. Bacteriol. , vol.194 , pp. 1024-1035
    • Göhler, A.K.1    Staab, A.2    Gabor, E.3    Homann, K.4    Klang, E.5    Kosfeld, A.6    Muus, J.E.7    Wulftange, J.S.8    Jahreis, K.9
  • 146
    • 84873476781 scopus 로고    scopus 로고
    • Membrane sequestration by the EIIB domain of the mannitol permease MtlA activates the Bacillus subtilis mtl operon regulator MtlR
    • Bouraoui H, Ventroux M, Noirot-Gros M-F, Deutscher J, Joyet P. 2013. Membrane sequestration by the EIIB domain of the mannitol permease MtlA activates the Bacillus subtilis mtl operon regulator MtlR. Mol. Microbiol. 87:789-801. http://dx.doi.org/10.1111/mmi.12131.
    • (2013) Mol. Microbiol. , vol.87 , pp. 789-801
    • Bouraoui, H.1    Ventroux, M.2    Noirot-Gros, M.-F.3    Deutscher, J.4    Joyet, P.5
  • 148
    • 77955499215 scopus 로고    scopus 로고
    • Localization of the substrate- binding site in the homodimeric mannitol transporter, EIImtl, of Escherichia coli
    • Opacić M, Vos EP, Hesp BH, Broos J. 2010. Localization of the substrate- binding site in the homodimeric mannitol transporter, EIImtl, of Escherichia coli. J. Biol. Chem. 285:25324-25331. http://dx.doi.org/10 .1074/jbc.M110.122523.
    • (2010) J. Biol. Chem. , vol.285 , pp. 25324-25331
    • Opacić, M.1    Vos, E.P.2    Hesp, B.H.3    Broos, J.4
  • 149
    • 80054691607 scopus 로고    scopus 로고
    • Regulation of mtl operon promoter of Bacillus subtilis: Requirements of its use in expression vectors
    • Heravi KM, Wenzel M, Altenbuchner J. 2011. Regulation of mtl operon promoter of Bacillus subtilis: requirements of its use in expression vectors. Microb. Cell Fact. 10:83. http://dx.doi.org/10.1186/1475-2859-10-83.
    • (2011) Microb. Cell Fact. , vol.10 , pp. 83
    • Heravi, K.M.1    Wenzel, M.2    Altenbuchner, J.3
  • 150
    • 77950669373 scopus 로고    scopus 로고
    • The major PEP-phosphotransferase systems (PTSs) for glucose, mannose and cellobiose of Listeria monocytogenes, and their significance for extra- and intracellular growth
    • Stoll R, Goebel W. 2010. The major PEP-phosphotransferase systems (PTSs) for glucose, mannose and cellobiose of Listeria monocytogenes, and their significance for extra- and intracellular growth. Microbiology 156:1069-1083. http://dx.doi.org/10.1099/mic.0.034934-0.
    • (2010) Microbiology , vol.156 , pp. 1069-1083
    • Stoll, R.1    Goebel, W.2
  • 151
    • 77954001197 scopus 로고    scopus 로고
    • The phosphoenolpyruvate phosphotransferase system regulates Vibrio cholerae biofilm formation through multiple independent pathways
    • Houot L, Chang S, Pickering BS, Absalon C, Watnick PI. 2010. The phosphoenolpyruvate phosphotransferase system regulates Vibrio cholerae biofilm formation through multiple independent pathways. J. Bacteriol. 192:3055-3067. http://dx.doi.org/10.1128/JB.00213-10.
    • (2010) J. Bacteriol. , vol.192 , pp. 3055-3067
    • Houot, L.1    Chang, S.2    Pickering, B.S.3    Absalon, C.4    Watnick, P.I.5
  • 152
    • 84880674851 scopus 로고    scopus 로고
    • Mannitol and the mannitolspecific enzyme IIB subunit activate Vibrio cholerae biofilm formation
    • Ymele-Leki P, Houot L, Watnick PI. 2013. Mannitol and the mannitolspecific enzyme IIB subunit activate Vibrio cholerae biofilm formation. Appl. Environ. Microbiol. 79:4675-4683. http://dx.doi.org/10.1128 /AEM.01184-13.
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 4675-4683
    • Ymele-Leki, P.1    Houot, L.2    Watnick, P.I.3
  • 153
    • 8544261105 scopus 로고    scopus 로고
    • Enolase in the RNA degradosome plays a crucial role in the rapid decay of glucose transporter mRNA in the response to phosphosugar stress in Escherichia coli
    • Morita T, Kawamoto H, Mizota T, Inada T, Aiba H. 2004. Enolase in the RNA degradosome plays a crucial role in the rapid decay of glucose transporter mRNA in the response to phosphosugar stress in Escherichia coli. Mol. Microbiol. 54:1063-1075. http://dx.doi.org/10.1111/j.1365-2958.2004.04329.x.
    • (2004) Mol. Microbiol. , vol.54 , pp. 1063-1075
    • Morita, T.1    Kawamoto, H.2    Mizota, T.3    Inada, T.4    Aiba, H.5
  • 154
    • 80955179563 scopus 로고    scopus 로고
    • The phosphoenolpyruvate-dependent glucose-phosphotransferase system from Escherichia coli K-12 as the center of a network regulating carbohydrate flux in the cell
    • Gabor E, Göhler AK, Kosfeld A, Staab A, Kremling A, Jahreis K. 2011. The phosphoenolpyruvate-dependent glucose-phosphotransferase system from Escherichia coli K-12 as the center of a network regulating carbohydrate flux in the cell. Eur. J. Cell Biol. 90:711-720. http://dx.doi .org/10.1016/j.ejcb. 2011.04.002.
    • (2011) Eur. J. Cell Biol. , vol.90 , pp. 711-720
    • Gabor, E.1    Göhler, A.K.2    Kosfeld, A.3    Staab, A.4    Kremling, A.5    Jahreis, K.6
  • 155
    • 84893482882 scopus 로고    scopus 로고
    • Nutritional control of antibiotic resistance via an interface between the phosphotransferase system and a two-component signaling system
    • 25 November
    • Snyder H, Kellogg SL, Skarda LM, Little JL, Kristich CJ. 25 November 2013. Nutritional control of antibiotic resistance via an interface between the phosphotransferase system and a two-component signaling system. Antimicrob. Agents Chemother. http://dx.doi.org/10.1128/AAC.01919-13.
    • (2013) Antimicrob. Agents Chemother
    • Snyder, H.1    Kellogg, S.L.2    Skarda, L.M.3    Little, J.L.4    Kristich, C.J.5
  • 156
    • 0030724011 scopus 로고    scopus 로고
    • High affinity binding and allosteric regulation of Escherichia coli glycogen phosphorylase by the histidine phosphocarrier protein, HPr
    • Seok Y-J, Sondej M, Badawi P, Lewis MS, Briggs MC, Jaffe H, Peterkofsky A. 1997. High affinity binding and allosteric regulation of Escherichia coli glycogen phosphorylase by the histidine phosphocarrier protein, HPr. J. Biol. Chem. 272:26511-26521. http://dx.doi.org/10.1074 /jbc.272.42.26511.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26511-26521
    • Seok, Y.-J.1    Sondej, M.2    Badawi, P.3    Lewis, M.S.4    Briggs, M.C.5    Jaffe, H.6    Peterkofsky, A.7
  • 157
    • 0347670033 scopus 로고    scopus 로고
    • Regulation of glycogen concentration by the histidine-containing phosphocarrier protein HPr in Escherichia coli
    • Koo BM, Seok Y-J. 2001. Regulation of glycogen concentration by the histidine-containing phosphocarrier protein HPr in Escherichia coli. J. Microbiol. 39:24-30.
    • (2001) J. Microbiol. , vol.39 , pp. 24-30
    • Koo, B.M.1    Seok, Y.-J.2
  • 158
    • 80054839420 scopus 로고    scopus 로고
    • Crh, the paralogue of the phosphocarrier protein HPr, controls the methylglyoxal bypass of glycolysis in Bacillus subtilis
    • Landmann JJ, Busse RA, Latz JH, Singh KD, Stülke J, Görke B. 2011. Crh, the paralogue of the phosphocarrier protein HPr, controls the methylglyoxal bypass of glycolysis in Bacillus subtilis. Mol. Microbiol. 82:770-787. http://dx.doi.org/10.1111/j.1365-2958.2011.07857.x.
    • (2011) Mol. Microbiol. , vol.82 , pp. 770-787
    • Landmann, J.J.1    Busse, R.A.2    Latz, J.H.3    Singh, K.D.4    Stülke, J.5    Görke, B.6
  • 159
    • 79958221467 scopus 로고    scopus 로고
    • Dephosphorylated NPr of the nitrogen PTS regulates lipid A biosynthesis by direct interaction with LpxD
    • Kim HJ, Lee CR, Kim M, Peterkofsky A, Seok YJ. 2011. Dephosphorylated NPr of the nitrogen PTS regulates lipid A biosynthesis by direct interaction with LpxD. Biochem. Biophys. Res. Commun. 409:556-561. http://dx.doi.org/10.1016/j. bbrc.2011.05.044.
    • (2011) Biochem. Biophys. Res. Commun. , vol.409 , pp. 556-561
    • Kim, H.J.1    Lee, C.R.2    Kim, M.3    Peterkofsky, A.4    Seok, Y.J.5
  • 160
    • 70249134273 scopus 로고    scopus 로고
    • Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis
    • Bartling CM, Raetz CR. 2009. Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis. Biochemistry 48:8672-8683. http://dx.doi.org/10.1021/bi901025v.
    • (2009) Biochemistry , vol.48 , pp. 8672-8683
    • Bartling, C.M.1    Raetz, C.R.2
  • 161
    • 84872236877 scopus 로고    scopus 로고
    • Bacterial chemotaxis: The early years of molecular studies
    • Hazelbauer GL. 2012. Bacterial chemotaxis: the early years of molecular studies. Annu. Rev. Microbiol. 66:285-303. http://dx.doi.org/10.1146 /annurev-micro-092611-150120.
    • (2012) Annu. Rev. Microbiol. , vol.66 , pp. 285-303
    • Hazelbauer, G.L.1
  • 162
    • 80054722813 scopus 로고    scopus 로고
    • A molecular mechanism of direction switching in the flagellar motor of Escherichia coli Proc
    • Paul K, Brunstetter D, Titen S, Blair DF. 2011. A molecular mechanism of direction switching in the flagellar motor of Escherichia coli Proc. Natl. Acad. Sci. U. S. A. 108:17171-17176. http://dx.doi.org/10.1073/pnas .1110111108.
    • (2011) Natl. Acad. Sci. U. S. A. , vol.108 , pp. 17171-17176
    • Paul, K.1    Brunstetter, D.2    Titen, S.3    Blair, D.F.4
  • 163
    • 0029616573 scopus 로고
    • Coupling of the phosphotransferase system and the methyl-accepting chemotaxis protein-dependent chemotaxis signaling pathways of Escherichia coli
    • Lux R, Jahreis K, Bettenbrock K, Parkinson JS, Lengeler JW. 1995. Coupling of the phosphotransferase system and the methyl-accepting chemotaxis protein-dependent chemotaxis signaling pathways of Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 92:11583-11587. http://dx.doi .org/10.1073/pnas.92.25. 11583.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 11583-11587
    • Lux, R.1    Jahreis, K.2    Bettenbrock, K.3    Parkinson, J.S.4    Lengeler, J.W.5
  • 164
    • 0031750695 scopus 로고    scopus 로고
    • Unique regulation of carbohydrate chemotaxis in Bacillus subtilis by the phosphoenolpyruvate-dependent phosphotransferase system and the methyl-accepting chemotaxis protein McpC
    • Garrity LF, Schiel SL, Merrill R, Reizer J, Saier MH, Jr, Ordal GW. 1998. Unique regulation of carbohydrate chemotaxis in Bacillus subtilis by the phosphoenolpyruvate-dependent phosphotransferase system and the methyl-accepting chemotaxis protein McpC. J. Bacteriol. 180:4475-4480.
    • (1998) J. Bacteriol. , vol.180 , pp. 4475-4480
    • Garrity, L.F.1    Schiel, S.L.2    Merrill, R.3    Reizer, J.4    Saier Jr., M.H.5    Ordal, G.W.6
  • 165
    • 0035877793 scopus 로고    scopus 로고
    • Evidence for direct interaction between enzyme INtr and aspartokinase to regulate bacterial oligopeptide transport
    • King ND, O'Brian MR. 2001. Evidence for direct interaction between enzyme INtr and aspartokinase to regulate bacterial oligopeptide transport. J. Biol. Chem. 276:21311-21316. http://dx.doi.org/10.1074/jbc .M101982200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21311-21316
    • King, N.D.1    O'brian, M.R.2
  • 166
    • 4544356004 scopus 로고    scopus 로고
    • Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P
    • Schumacher MA, Allen GS, Diel M, Seidel G, Hillen W, Brennan RG. 2004. Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P. Cell 118:731-741. http://dx .doi.org/10.1016/j. cell.2004.08.027.
    • (2004) Cell , vol.118 , pp. 731-741
    • Schumacher, M.A.1    Allen, G.S.2    Diel, M.3    Seidel, G.4    Hillen, W.5    Brennan, R.G.6
  • 167
    • 0036266647 scopus 로고    scopus 로고
    • The regulation of enzyme IIAGlc expression controls adenylate cyclase activity in Escherichia coli
    • Krin E, Sismeiro O, Danchin A, Bertin PN. 2002. The regulation of enzyme IIAGlc expression controls adenylate cyclase activity in Escherichia coli. Microbiology 148:1553-1559.
    • (2002) Microbiology , vol.148 , pp. 1553-1559
    • Krin, E.1    Sismeiro, O.2    Danchin, A.3    Bertin, P.N.4
  • 168
    • 79957667493 scopus 로고    scopus 로고
    • Protein expression dynamics during Escherichia coli glucose-lactose diauxie
    • Mostovenko E, Deelder AM, Palmblad M. 2011. Protein expression dynamics during Escherichia coli glucose-lactose diauxie. BMC Microbiol. 11:126. http://dx.doi.org/10.1186/1471-2180-11-126.
    • (2011) BMC Microbiol. , vol.11 , pp. 126
    • Mostovenko, E.1    Deelder, A.M.2    Palmblad, M.3
  • 169
    • 0027376662 scopus 로고
    • A lowered concentration of cAMP receptor protein caused by glucose is an important determinant for catabolite repression in Escherichia coli
    • Ishizuka H, Hanamura A, Kunimura T, Aiba H. 1993. A lowered concentration of cAMP receptor protein caused by glucose is an important determinant for catabolite repression in Escherichia coli. Mol. Microbiol. 10: 341-350. http://dx.doi.org/10.1111/j.1365-2958.1993.tb01960.x.
    • (1993) Mol. Microbiol. , vol.10 , pp. 341-350
    • Ishizuka, H.1    Hanamura, A.2    Kunimura, T.3    Aiba, H.4
  • 170
    • 0020470978 scopus 로고
    • Significance of -galactosidase repression in glucose inhibition of lactose utilization in Escherichia coli
    • Fraser ADE, Yamazaki H. 1982. Significance of -galactosidase repression in glucose inhibition of lactose utilization in Escherichia coli. Curr. Microbiol. 7:241-244. http://dx.doi.org/10.1007/BF01568806.
    • (1982) Curr. Microbiol. , vol.7 , pp. 241-244
    • Fraser, A.D.E.1    Yamazaki, H.2
  • 171
    • 33646570920 scopus 로고    scopus 로고
    • In vitro reconstitution of catabolite repression in Escherichia coli
    • Park Y-H, Lee BR, Seok Y-J, Peterkofsky A. 2006. In vitro reconstitution of catabolite repression in Escherichia coli. J. Biol. Chem. 281:6448-6454. http://dx.doi.org/10.1074/jbc.M512672200.
    • (2006) J. Biol. Chem. , vol.281 , pp. 6448-6454
    • Park, Y.-H.1    Lee, B.R.2    Seok, Y.-J.3    Peterkofsky, A.4
  • 172
    • 0037795504 scopus 로고    scopus 로고
    • The BglF sensor recruits the BglG transcription regulator to the membrane and releases it on stimulation
    • Lopian L, Nussbaum-Shochat A, O'Day-Kerstein K, Wright A, Amster-Choder O. 2003. The BglF sensor recruits the BglG transcription regulator to the membrane and releases it on stimulation. Proc. Natl. Acad. Sci. U. S. A. 100:7099-7104. http://dx.doi.org/10.1073 /pnas.1037608100.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 7099-7104
    • Lopian, L.1    Nussbaum-Shochat, A.2    O'day-Kerstein, K.3    Wright, A.4    Amster-Choder, O.5
  • 173
    • 84877962831 scopus 로고    scopus 로고
    • Dynamic localization of a transcription factor in Bacillus subtilis: The LicT antiterminator relocalizes in response to inducer availability
    • Rothe FM, Wrede C, Lehnik-Habrink M, Görke B, Stülke J. 2013. Dynamic localization of a transcription factor in Bacillus subtilis: the LicT antiterminator relocalizes in response to inducer availability. J. Bacteriol. 195:2146-2154. http://dx.doi.org/10.1128/JB.00117-13.
    • (2013) J. Bacteriol. , vol.195 , pp. 2146-2154
    • Rothe, F.M.1    Wrede, C.2    Lehnik-Habrink, M.3    Görke, B.4    Stülke, J.5
  • 174
    • 0036786814 scopus 로고    scopus 로고
    • Growing repertoire of AraC/XylS activators
    • Egan SM. 2002. Growing repertoire of AraC/XylS activators. J. Bacteriol. 184:5529-5532. http://dx.doi.org/10.1128/JB.184.20.5529-5532.2002.
    • (2002) J. Bacteriol. , vol.184 , pp. 5529-5532
    • Egan, S.M.1
  • 175
    • 70350493718 scopus 로고    scopus 로고
    • Transcriptional activator YesS is stimulated by histidine-phosphorylated HPr of the Bacillus subtilis phosphotransferase system
    • Poncet S, Soret M, Mervelet P, Deutscher J, Noirot P. 2009. Transcriptional activator YesS is stimulated by histidine-phosphorylated HPr of the Bacillus subtilis phosphotransferase system. J. Biol. Chem. 284: 28188-28197. http://dx.doi.org/10.1074/jbc.M109.046334.
    • (2009) J. Biol. Chem. , vol.284 , pp. 28188-28197
    • Poncet, S.1    Soret, M.2    Mervelet, P.3    Deutscher, J.4    Noirot, P.5
  • 176
    • 84899797306 scopus 로고    scopus 로고
    • Phosphorylation of HPr by HPr kinase in Gluconobacter oxydans 621H
    • 11 February
    • Zhang P, Ma Y, Wang F, Wei D. 11 February 2014. Phosphorylation of HPr by HPr kinase in Gluconobacter oxydans 621H. Protein Pept. Lett. http://dx.doi.org/10.2174/0929866521666140212111059.
    • (2014) Protein Pept. Lett
    • Zhang, P.1    Ma, Y.2    Wang, F.3    Wei, D.4
  • 177
    • 47549110972 scopus 로고    scopus 로고
    • Carbon catabolite repression in bacteria: Many ways to make the most out of nutrients
    • Görke B, Stülke J. 2008. Carbon catabolite repression in bacteria: many ways to make the most out of nutrients. Nat. Rev. Microbiol. 6:613-624. http://dx.doi.org/10.1038/nrmicro1932.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 613-624
    • Görke, B.1    Stülke, J.2
  • 178
    • 42049092081 scopus 로고    scopus 로고
    • The mechanisms of carbon catabolite repression in bacteria
    • Deutscher J. 2008. The mechanisms of carbon catabolite repression in bacteria. Curr. Opin. Microbiol. 11:87-93. http://dx.doi.org/10.1016/j .mib.2008.02.007.
    • (2008) Curr. Opin. Microbiol. , vol.11 , pp. 87-93
    • Deutscher, J.1
  • 179
    • 0028917215 scopus 로고
    • Protein kinase-dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in Gram-positive bacteria
    • Deutscher J, Küster E, Bergstedt U, Charrier V, Hillen W. 1995. Protein kinase-dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in Gram-positive bacteria. Mol. Microbiol. 15:1049-1053. http://dx.doi.org/10.1111/j.1365-2958.1995.tb02280.x.
    • (1995) Mol. Microbiol. , vol.15 , pp. 1049-1053
    • Deutscher, J.1    Küster, E.2    Bergstedt, U.3    Charrier, V.4    Hillen, W.5
  • 180
    • 0028827880 scopus 로고
    • Specific recognition of the Bacillus subtilis gnt cis-acting catabolite-responsive element by a protein complex formed between CcpA and seryl-phosphorylated HPr
    • Fujita Y, Miwa Y, Galinier A, Deutscher J. 1995. Specific recognition of the Bacillus subtilis gnt cis-acting catabolite-responsive element by a protein complex formed between CcpA and seryl-phosphorylated HPr. Mol. Microbiol. 17:953-960. http://dx.doi.org/10.1111/j.1365-2958.1995 .mmi-17050953.x.
    • (1995) Mol. Microbiol. , vol.17 , pp. 953-960
    • Fujita, Y.1    Miwa, Y.2    Galinier, A.3    Deutscher, J.4
  • 184
    • 0032955592 scopus 로고    scopus 로고
    • Phosphorylation of HPr and Crh by HprK, early steps in the catabolite repression signalling pathway for the Bacillus subtilis levanase operon
    • Martin-Verstraete I, Deutscher J, Galinier A. 1999. Phosphorylation of HPr and Crh by HprK, early steps in the catabolite repression signalling pathway for the Bacillus subtilis levanase operon. J. Bacteriol. 181:2966-2969.
    • (1999) J. Bacteriol. , vol.181 , pp. 2966-2969
    • Martin-Verstraete, I.1    Deutscher, J.2    Galinier, A.3
  • 185
    • 33846636980 scopus 로고    scopus 로고
    • Interaction of GapA with HPr and its homologue, Crh: Novel levels of regulation of a key step of glycolysis in Bacillus subtilis?
    • Pompeo F, Luciano J, Galinier A. 2007. Interaction of GapA with HPr and its homologue, Crh: novel levels of regulation of a key step of glycolysis in Bacillus subtilis?. J. Bacteriol. 189:1154-1157. http://dx.doi.org/10 .1128/JB.01575-06.
    • (2007) J. Bacteriol. , vol.189 , pp. 1154-1157
    • Pompeo, F.1    Luciano, J.2    Galinier, A.3
  • 187
    • 78650097558 scopus 로고    scopus 로고
    • Glucose-dependent activation of Bacillus anthracis toxin gene expression and virulence requires the carbon catabolite protein CcpA
    • Chiang C, Bongiorni C, Perego M. 2011. Glucose-dependent activation of Bacillus anthracis toxin gene expression and virulence requires the carbon catabolite protein CcpA. J. Bacteriol. 193:52-62. http://dx.doi .org/10.1128/JB.01656-09.
    • (2011) J. Bacteriol. , vol.193 , pp. 52-62
    • Chiang, C.1    Bongiorni, C.2    Perego, M.3
  • 188
    • 0034100838 scopus 로고    scopus 로고
    • Enzyme i and HPr from Lactobacillus casei: Their role in sugar transport, carbon catabolite repression and inducer exclusion
    • Viana R, Monedero V, Dossonnet V, Vadeboncoeur C, Pérez- Martínez G, Deutscher J. 2000. Enzyme I and HPr from Lactobacillus casei: their role in sugar transport, carbon catabolite repression and inducer exclusion. Mol. Microbiol. 36:570-584. http://dx.doi.org/10.1046 /j.1365-2958.2000.01862.x.
    • (2000) Mol. Microbiol. , vol.36 , pp. 570-584
    • Viana, R.1    Monedero, V.2    Dossonnet, V.3    Vadeboncoeur, C.4    Pérez- Martínez, G.5    Deutscher, J.6
  • 189
    • 0033996770 scopus 로고    scopus 로고
    • Phosphorylation of HPr by the bifunctional HPr kinase/ P-Ser-HPr phosphatase from Lactobacillus casei controls catabolite repression and inducer exclusion but not inducer expulsion
    • Dossonnet V, Monedero V, Zagorec M, Galinier A, Pérez- Martínez G, Deutscher J. 2000. Phosphorylation of HPr by the bifunctional HPr kinase/ P-Ser-HPr phosphatase from Lactobacillus casei controls catabolite repression and inducer exclusion but not inducer expulsion. J. Bacteriol. 182: 2582-2590. http://dx.doi.org/10.1128/JB.182.9.2582-2590.2000.
    • (2000) J. Bacteriol. , vol.182 , pp. 2582-2590
    • Dossonnet, V.1    Monedero, V.2    Zagorec, M.3    Galinier, A.4    Pérez- Martínez, G.5    Deutscher, J.6
  • 190
    • 0035026054 scopus 로고    scopus 로고
    • Regulatory functions of serine-46-phosphorylated HPr in Lactococcus lactis
    • Monedero V, Kuipers OP, Jamet E, Deutscher J. 2001. Regulatory functions of serine-46-phosphorylated HPr in Lactococcus lactis. J. Bacteriol. 183:3391-3398. http://dx.doi.org/10.1128/JB.183.11.3391-3398 .2001.
    • (2001) J. Bacteriol. , vol.183 , pp. 3391-3398
    • Monedero, V.1    Kuipers, O.P.2    Jamet, E.3    Deutscher, J.4
  • 192
    • 39649109260 scopus 로고    scopus 로고
    • Maltose transport in Lactobacillus casei and its regulation by inducer exclusion
    • Monedero V, Yebra MJ, Poncet S, Deutscher J. 2008. Maltose transport in Lactobacillus casei and its regulation by inducer exclusion. Res. Microbiol. 159:94-102. http://dx.doi.org/10.1016/j.resmic.2007.10.002.
    • (2008) Res. Microbiol. , vol.159 , pp. 94-102
    • Monedero, V.1    Yebra, M.J.2    Poncet, S.3    Deutscher, J.4
  • 193
    • 0020553970 scopus 로고
    • Mechanism of inducer expulsion in Streptococcus pyogenes: A two-step process activated by ATP
    • Reizer J, Novotny MJ, Panos C, Saier MH, Jr. 1983. Mechanism of inducer expulsion in Streptococcus pyogenes: a two-step process activated by ATP. J. Bacteriol. 156:354-361.
    • (1983) J. Bacteriol. , vol.156 , pp. 354-361
    • Reizer, J.1    Novotny, M.J.2    Panos, C.3    Saier Jr., M.H.4
  • 194
    • 0019214568 scopus 로고
    • Regulation of -galactoside phosphate accumulation in Streptococcus pyogenes by an expulsion mechanism
    • Reizer J, Panos C. 1980. Regulation of -galactoside phosphate accumulation in Streptococcus pyogenes by an expulsion mechanism. Proc. Natl. Acad. Sci. U. S. A. 77:5497-5501. http://dx.doi.org/10.1073/pnas.77 .9.5497.
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 5497-5501
    • Reizer, J.1    Panos, C.2
  • 195
    • 0020450746 scopus 로고
    • Novel phosphoenolpyruvatedependent futile cycle in Streptococcus lactis: 2-deoxyglucose uncouples energy production from growth
    • Thompson J, Chassy BM. 1982. Novel phosphoenolpyruvatedependent futile cycle in Streptococcus lactis: 2-deoxyglucose uncouples energy production from growth. J. Bacteriol. 151:1454-1465.
    • (1982) J. Bacteriol. , vol.151 , pp. 1454-1465
    • Thompson, J.1    Chassy, B.M.2
  • 196
    • 0029863334 scopus 로고    scopus 로고
    • Inducer expulsion and the occurrence of an HPr(Ser-P)-activated sugar phosphate phosphatase in Enterococcus faecalis and Streptococcus pyogenes
    • Ye J-J, Minarcik J, Saier MH, Jr. 1996. Inducer expulsion and the occurrence of an HPr(Ser-P)-activated sugar phosphate phosphatase in Enterococcus faecalis and Streptococcus pyogenes. Microbiology 142:585-592. http://dx.doi.org/10.1099/13500872-142-3-585.
    • (1996) Microbiology , vol.142 , pp. 585-592
    • Ye, J.-J.1    Minarcik, J.2    Saier Jr., M.H.3
  • 197
    • 0029054032 scopus 로고
    • Purification and characterization of a small membrane-associated sugar phosphate phosphatase that is allosterically activated by HPr(Ser(P)) of the phosphotransferase system in Lactococcus lactis
    • Ye J-J, Saier MH, Jr. 1995. Purification and characterization of a small membrane-associated sugar phosphate phosphatase that is allosterically activated by HPr(Ser(P)) of the phosphotransferase system in Lactococcus lactis. J. Biol. Chem. 270:16740-16744. http://dx.doi.org/10.1074/jbc .270.28.16740.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16740-16744
    • Ye, J.-J.1    Saier Jr., M.H.2
  • 198
    • 0028842580 scopus 로고
    • Properties of two sugarphosphate phosphatases from Streptococcus bovis and their potential involvement in inducer expulsion
    • Cook GM, Ye J-J, Russell JB, Saier MH, Jr. 1995. Properties of two sugarphosphate phosphatases from Streptococcus bovis and their potential involvement in inducer expulsion. J. Bacteriol. 177:7007-7009.
    • (1995) J. Bacteriol. , vol.177 , pp. 7007-7009
    • Cook, G.M.1    Ye, J.-J.2    Russell, J.B.3    Saier Jr., M.H.4
  • 199
    • 0007402076 scopus 로고
    • ATP-dependent phosphorylation of serine-46 in the phosphocarrier protein HPr regulates lactose/ H+ symport in Lactobacillus brevis
    • Ye J-J, Reizer J, Cui X, Saier MH, Jr. 1994. ATP-dependent phosphorylation of serine-46 in the phosphocarrier protein HPr regulates lactose/ H+ symport in Lactobacillus brevis. Proc. Natl. Acad. Sci. U. S. A. 91:3102-3106. http://dx.doi.org/10.1073/pnas.91.8.3102.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 3102-3106
    • Ye, J.-J.1    Reizer, J.2    Cui, X.3    Saier Jr., M.H.4
  • 200
    • 0035036090 scopus 로고    scopus 로고
    • Genes involved in control of galactose uptake in Lactobacillus brevis and reconstitution of the regulatory system in Bacillus subtilis
    • Djordjevic GM, Tchieu JH, Saier MH, Jr. 2001. Genes involved in control of galactose uptake in Lactobacillus brevis and reconstitution of the regulatory system in Bacillus subtilis. J. Bacteriol. 183:3224-3236. http://dx.doi.org/10. 1128/JB.183.10.3224-3236.2001.
    • (2001) J. Bacteriol. , vol.183 , pp. 3224-3236
    • Djordjevic, G.M.1    Tchieu, J.H.2    Saier Jr., M.H.3
  • 201
    • 0014104790 scopus 로고
    • Carbohydrate transport in Staphylococcus aureus.V. The accumulation of phosphorylated carbohydrate derivatives, and evidence for a new enzyme-splitting lactose phosphate
    • Hengstenberg W, Egan JB, Morse ML. 1967. Carbohydrate transport in Staphylococcus aureus. V. The accumulation of phosphorylated carbohydrate derivatives, and evidence for a new enzyme-splitting lactose phosphate. Proc. Natl. Acad. Sci. U. S. A. 58:274-279.
    • (1967) Proc. Natl. Acad. Sci. U. S. A. , vol.58 , pp. 274-279
    • Hengstenberg, W.1    Egan, J.B.2    Morse, M.L.3
  • 204
    • 0014561151 scopus 로고
    • Phosphotransferase system of Staphylococcus aureus: Its requirement for the accumulation and metabolism of galactosides
    • Hengstenberg W, Penberthy WK, Hill KL, Morse ML. 1969. Phosphotransferase system of Staphylococcus aureus: its requirement for the accumulation and metabolism of galactosides. J. Bacteriol. 99:383-388.
    • (1969) J. Bacteriol. , vol.99 , pp. 383-388
    • Hengstenberg, W.1    Penberthy, W.K.2    Hill, K.L.3    Morse, M.L.4
  • 206
    • 0018612938 scopus 로고
    • Pentitol metabolism in Lactobacillus casei
    • London J, Chace NM. 1979. Pentitol metabolism in Lactobacillus casei. J. Bacteriol. 140:949-954.
    • (1979) J. Bacteriol. , vol.140 , pp. 949-954
    • London, J.1    Chace, N.M.2
  • 207
    • 84877983554 scopus 로고    scopus 로고
    • Utilization of D-ribitol by Lactobacillus casei BL23 requires a mannose-type phosphotransferase system and three catabolic enzymes
    • Bourand A, Yebra MJ, Boël G, Mazé A, Deutscher J. 2013. Utilization of D-ribitol by Lactobacillus casei BL23 requires a mannose-type phosphotransferase system and three catabolic enzymes. J. Bacteriol. 195: 2652-2661. http://dx.doi.org/10.1128/JB.02276-12.
    • (2013) J. Bacteriol. , vol.195 , pp. 2652-2661
    • Bourand, A.1    Yebra, M.J.2    Boël, G.3    Mazé, A.4    Deutscher, J.5
  • 208
    • 0037378580 scopus 로고    scopus 로고
    • The ascorbate transporter of Escherichia coli
    • Zhang ZG, Aboulwafa M, Smith MH, Saier MH, Jr. 2003. The ascorbate transporter of Escherichia coli. J. Bacteriol. 185:2243-2250. http://dx .doi.org/10.1128/JB.185.7.2243-2250.2003.
    • (2003) J. Bacteriol. , vol.185 , pp. 2243-2250
    • Zhang, Z.G.1    Aboulwafa, M.2    Smith, M.H.3    Saier Jr., M.H.4
  • 209
    • 34247892340 scopus 로고    scopus 로고
    • A phosphoenolpyruvatedependent phosphotransferase system is the principal maltose transporter in Streptococcus mutans
    • Webb AJ, Homer KA, Hosie AH. 2007. A phosphoenolpyruvatedependent phosphotransferase system is the principal maltose transporter in Streptococcus mutans. J. Bacteriol. 189:3322-3327. http://dx.doi .org/10.1128/JB.01633-06.
    • (2007) J. Bacteriol. , vol.189 , pp. 3322-3327
    • Webb, A.J.1    Homer, K.A.2    Hosie, A.H.3
  • 211
    • 52649125713 scopus 로고    scopus 로고
    • The Ser/Thr/Tyr phosphoproteome of Lactococcus lactis IL1403 reveals multiply phosphorylated proteins
    • Soufi B, Gnad F, Jensen PR, Petranovi D, Mann M, Mijakovic I, Macek B. 2008. The Ser/Thr/Tyr phosphoproteome of Lactococcus lactis IL1403 reveals multiply phosphorylated proteins. Proteomics 8:3486-3493. http://dx.doi.org/10. 1002/pmic.200800069.
    • (2008) Proteomics , vol.8 , pp. 3486-3493
    • Soufi, B.1    Gnad, F.2    Jensen, P.R.3    Petranovi, D.4    Mann, M.5    Mijakovic, I.6    Macek, B.7
  • 212
    • 34247325212 scopus 로고    scopus 로고
    • The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis
    • Macek B, Mijakovic I, Olse JV, Gnad F, Kumar C, Jensen PR, Mann M. 2007. The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol. Cell. Proteomics 6:697-707. http://dx .doi.org/10.1074/mcp. M600464-MCP200.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 697-707
    • Macek, B.1    Mijakovic, I.2    Olse, J.V.3    Gnad, F.4    Kumar, C.5    Jensen, P.R.6    Mann, M.7
  • 213
    • 84856611249 scopus 로고    scopus 로고
    • Analysis of the serine/threonine/tyrosine phosphoproteome of the pathogenic bacterium Listeria monocytogenes reveals phosphorylated proteins related to virulence
    • Misra SK, Milohanic E, Francine A, Mijakovic I, Deutscher J, Monnet V, Henry C. 2011. Analysis of the serine/threonine/tyrosine phosphoproteome of the pathogenic bacterium Listeria monocytogenes reveals phosphorylated proteins related to virulence. Proteomics 11:4155-4165. http://dx.doi.org/10.1002/pmic. 201100259.
    • (2011) Proteomics , vol.11 , pp. 4155-4165
    • Misra, S.K.1    Milohanic, E.2    Francine, A.3    Mijakovic, I.4    Deutscher, J.5    Monnet, V.6    Henry, C.7
  • 214
    • 77953160473 scopus 로고    scopus 로고
    • The phosphoproteome of the minimal bacterium Mycoplasma pneumoniae: Analysis of the complete known Ser/Thr kinome suggests the existence of novel kinases
    • Schmidl SR, Gronau K, Pietack N, Hecker M, Becher D, Stülke J. 2010. The phosphoproteome of the minimal bacterium Mycoplasma pneumoniae: analysis of the complete known Ser/Thr kinome suggests the existence of novel kinases. Mol. Cell. Proteomics 9:1228-1242. http://dx .doi.org/10.1074/mcp.M900267-MCP200.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1228-1242
    • Schmidl, S.R.1    Gronau, K.2    Pietack, N.3    Hecker, M.4    Becher, D.5    Stülke, J.6
  • 216
    • 73649133664 scopus 로고    scopus 로고
    • Phosphoproteomic analysis reveals the multiple roles of phosphorylation in pathogenic bacterium Streptococcus pneumoniae
    • Sun X, Ge F, Xiao CL, Yin XF, Ge R, Zhang LH, He QY. 2010. Phosphoproteomic analysis reveals the multiple roles of phosphorylation in pathogenic bacterium Streptococcus pneumoniae. J. Proteome Res. 9:275-282. http://dx.doi.org/10.1021/pr900612v.
    • (2010) J. Proteome Res. , vol.9 , pp. 275-282
    • Sun, X.1    Ge, F.2    Xiao, C.L.3    Yin, X.F.4    Ge, R.5    Zhang, L.H.6    He, Q.Y.7
  • 217
    • 75149190104 scopus 로고    scopus 로고
    • Phosphoproteomics of Klebsiella pneumoniae NTUH-K2044 reveals a tight link between tyrosine phosphorylation and virulence
    • Lin MH, Hsu TL, Lin SY, Pan YJ, Jan JT, Wang JT, Khoo KH, Wu SH. 2009. Phosphoproteomics of Klebsiella pneumoniae NTUH-K2044 reveals a tight link between tyrosine phosphorylation and virulence. Mol. Cell. Proteomics 8:2613-2623. http://dx.doi.org/10.1074/mcp.M900276 -MCP200.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2613-2623
    • Lin, M.H.1    Hsu, T.L.2    Lin, S.Y.3    Pan, Y.J.4    Jan, J.T.5    Wang, J.T.6    Khoo, K.H.7    Wu, S.H.8
  • 218
    • 0027207045 scopus 로고
    • Expression of listeriolysin and phosphatidylinositol- specific phospholipase C is repressed by the plant-derived molecule cellobiose in Listeria monocytogenes
    • Park SF, Kroll RG. 1993. Expression of listeriolysin and phosphatidylinositol- specific phospholipase C is repressed by the plant-derived molecule cellobiose in Listeria monocytogenes. Mol. Microbiol. 8:653-661. http://dx.doi.org/10.1111/j.1365-2958.1993.tb01609.x.
    • (1993) Mol. Microbiol. , vol.8 , pp. 653-661
    • Park, S.F.1    Kroll, R.G.2
  • 219
    • 0031024403 scopus 로고    scopus 로고
    • Carbonsource regulation of virulence gene expression in Listeria monocytogenes
    • Milenbachs AA, Brown DP, Moors M, Youngman P. 1997. Carbonsource regulation of virulence gene expression in Listeria monocytogenes. Mol. Microbiol. 23:1075-1085. http://dx.doi.org/10.1046/j.1365-2958 .1997.2711634.x.
    • (1997) Mol. Microbiol. , vol.23 , pp. 1075-1085
    • Milenbachs, A.A.1    Brown, D.P.2    Moors, M.3    Youngman, P.4
  • 220
    • 30744462545 scopus 로고    scopus 로고
    • How seryl-phosphorylated HPr inhibits PrfA, a transcription activator of Listeria monocytogenes virulence genes
    • Herro R, Poncet S, Cossart P, Buchrieser C, Gouin E, Glaser P, Deutscher J. 2005. How seryl-phosphorylated HPr inhibits PrfA, a transcription activator of Listeria monocytogenes virulence genes. J. Mol. Microbiol. Biotechnol. 9:224-234. http://dx.doi.org/10.1159/000089650.
    • (2005) J. Mol. Microbiol. Biotechnol. , vol.9 , pp. 224-234
    • Herro, R.1    Poncet, S.2    Cossart, P.3    Buchrieser, C.4    Gouin, E.5    Glaser, P.6    Deutscher, J.7
  • 221
    • 33846254003 scopus 로고    scopus 로고
    • Interference of components of the phosphoenolpyruvate phosphotransferase system with the central virulence gene regulator PrfA of Listeria monocytogenes
    • http://dx.doi.org/10.1128/JB.00972-06
    • Mertins S, Joseph B, Goetz M, Ecke R, Seidel G, Sprehe M, Hillen W, Goebel W, Müller-Altrock S. 2007. Interference of components of the phosphoenolpyruvate phosphotransferase system with the central virulence gene regulator PrfA of Listeria monocytogenes. J. Bacteriol. 189:473-490. http://dx.doi.org/10.1128/JB.00972-06.
    • (2007) J. Bacteriol. , vol.189 , pp. 473-490
    • Mertins, S.1    Joseph, B.2    Goetz, M.3    Ecke, R.4    Seidel, G.5    Sprehe, M.6    Hillen, W.7    Goebel, W.8    Müller-Altrock, S.9


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