메뉴 건너뛰기




Volumn 9, Issue 3-4, 2006, Pages 224-234

How seryl-phosphorylated HPr inhibits PrfA, a transcription activator of Listeria monocytogenes virulence genes

Author keywords

Catabolite repression; HPr kinase phosphorylase; Listeria monocytogenes; Phosphoenolpyruvate:carbohydrate phosphotransferase system

Indexed keywords

ALANINE; BETA GALACTOSIDASE; GLYCOSIDASE; HISTIDINE 15; HISTIDINE DERIVATIVE; PHOSPHOENOLPYRUVATE; PHOSPHOTRANSFERASE; PROTEIN PSPAC; SERINE 46; SERINE DERIVATIVE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR PRFA; UNCLASSIFIED DRUG;

EID: 30744462545     PISSN: 14641801     EISSN: None     Source Type: Journal    
DOI: 10.1159/000089650     Document Type: Article
Times cited : (56)

References (48)
  • 1
    • 0031785753 scopus 로고    scopus 로고
    • A homolog of CcpA mediates catabolite control in Listeria monocytogenes but not carbon source regulation of virulence genes
    • Behari, J., Youngman, P. 1998. A homolog of CcpA mediates catabolite control in Listeria monocytogenes but not carbon source regulation of virulence genes. J Bacteriol 180:6316-6324.
    • (1998) J Bacteriol , vol.180 , pp. 6316-6324
    • Behari, J.1    Youngman, P.2
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0032839731 scopus 로고    scopus 로고
    • The bvr locus of Listeria monocytogenes mediates virulence gene repression by β-glucosides
    • Brehm, K., Ripio, M.T., Kreft, J., Vazquez-Boland, J.A. 1999. The bvr locus of Listeria monocytogenes mediates virulence gene repression by β-glucosides. J Bacteriol 181:5024-5032.
    • (1999) J Bacteriol , vol.181 , pp. 5024-5032
    • Brehm, K.1    Ripio, M.T.2    Kreft, J.3    Vazquez-Boland, J.A.4
  • 4
    • 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.
    • (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
  • 5
    • 0032900603 scopus 로고    scopus 로고
    • Mutational analysis of the role of HPr in Listeria monocytogenes
    • Christensen, D.P., Benson, A.K., Hutkins, R.W. 1999. Mutational analysis of the role of HPr in Listeria monocytogenes. Appl Environ Microbiol 65:2112-2115.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 2112-2115
    • Christensen, D.P.1    Benson, A.K.2    Hutkins, R.W.3
  • 6
    • 30744478198 scopus 로고    scopus 로고
    • Role of protein phosphorylation on serine/threonine and tyrosine in the virulence of bacterial pathogens
    • Cozzone, A.J. 2005. Role of protein phosphorylation on serine/threonine and tyrosine in the virulence of bacterial pathogens. J Mol Biol Biotechnol 9:198-213.
    • (2005) J Mol Biol Biotechnol , vol.9 , pp. 198-213
    • Cozzone, A.J.1
  • 7
    • 0035011826 scopus 로고    scopus 로고
    • Phosphotransfer functions of mutated Bacillus subtilis HPr-like protein Crh carrying a histidine in the active site
    • Darbon, E., Galinier, A., Le Coq, D., Deutscher, J. 2001. Phosphotransfer functions of mutated Bacillus subtilis HPr-like protein Crh carrying a histidine in the active site. J Mol Microbiol Biotechnol 3:439-444.
    • (2001) J Mol Microbiol Biotechnol , vol.3 , pp. 439-444
    • Darbon, E.1    Galinier, A.2    Le Coq, D.3    Deutscher, J.4
  • 8
    • 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.
    • (2002) Mol Microbiol , vol.43 , pp. 1039-1052
    • Darbon, E.1    Servant, P.2    Poncet, S.3    Deutscher, J.4
  • 9
    • 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.
    • (1984) FEMS Microbiol Lett , vol.23 , pp. 157-162
    • Deutscher, J.1    Engelmann, R.2
  • 11
    • 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.
    • (1995) Mol Microbiol , vol.15 , pp. 1049-1053
    • Deutscher, J.1    Küster, E.2    Bergstedt, U.3    Charrier, V.4    Hillen, W.5
  • 12
    • 0028364161 scopus 로고
    • Loss of protein kinase-catalyzed phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, by mutation of the ptsH gene confers catabolite repression resistance to several catabolic genes of Bacillus subtilis
    • Deutscher, J., Reizer, J., Fischer, C., Galinier, A., Saier, M.H. Jr., Steinmetz, M. 1994. Loss of protein kinase-catalyzed phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, by mutation of the ptsH gene confers catabolite repression resistance to several catabolic genes of Bacillus subtilis. J Bacteriol 176:3336-3344.
    • (1994) J Bacteriol , vol.176 , pp. 3336-3344
    • Deutscher, J.1    Reizer, J.2    Fischer, C.3    Galinier, A.4    Saier Jr., M.H.5    Steinmetz, M.6
  • 13
    • 0020851355 scopus 로고
    • ATP-dependent protein kinase-catalyzed phosphorylation of a seryl residue in HPr, a phosphate carrier protein of the phosphotransferase system in Streptococcus pyogenes
    • USA
    • Deutscher, J., Saier Jr, M.H. 1983. ATP-dependent protein kinase-catalyzed phosphorylation of a seryl residue in HPr, a phosphate carrier protein of the phosphotransferase system in Streptococcus pyogenes. Proc Natl Acad Sci USA 80:6790-6794.
    • (1983) Proc Natl Acad Sci , vol.80 , pp. 6790-6794
    • Deutscher, J.1    Saier Jr., M.H.2
  • 14
    • 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.
    • (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
  • 16
    • 17144398027 scopus 로고    scopus 로고
    • The mutation G145S in PrfA, a key virulence regulator of Listeria monocytogenes, increases DNA-binding affinity by stabilizing the HTH motif
    • Eiting, M., Hagelüken, G., Schubert, W.D., Heinz, D.W. 2005. The mutation G145S in PrfA, a key virulence regulator of Listeria monocytogenes, increases DNA-binding affinity by stabilizing the HTH motif. Mol Microbiol 56:433-446.
    • (2005) Mol Microbiol , vol.56 , pp. 433-446
    • Eiting, M.1    Hagelüken, G.2    Schubert, W.D.3    Heinz, D.W.4
  • 17
    • 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.
    • (1995) Mol Microbiol , vol.17 , pp. 953-960
    • Fujita, Y.1    Miwa, Y.2    Galinier, A.3    Deutscher, J.4
  • 20
    • 3242814591 scopus 로고    scopus 로고
    • Catabolite repression and virulence gene expression in Listeria monocytogenes
    • Gilbreth, S.E., Benson, A.K., Hutkins, R.W. 2004. Catabolite repression and virulence gene expression in Listeria monocytogenes. Curr Microbiol 49:95-98.
    • (2004) Curr Microbiol , vol.49 , pp. 95-98
    • Gilbreth, S.E.1    Benson, A.K.2    Hutkins, R.W.3
  • 21
    • 0034602291 scopus 로고    scopus 로고
    • Phosphorylation state of HPr determines the level of expression and the extent of phosphorylation of the lactose transport protein of Streptococcus thermophilus
    • Gunnewijk, M.G.W., Poolman, B. 2000. Phosphorylation state of HPr determines the level of expression and the extent of phosphorylation of the lactose transport protein of Streptococcus thermophilus. J Biol Chem 275:34073-34079.
    • (2000) J Biol Chem , vol.275 , pp. 34073-34079
    • Gunnewijk, M.G.W.1    Poolman, B.2
  • 22
    • 0025840353 scopus 로고
    • Genetic analysis in Bacillus subtilis
    • Hoch, J.A. 1991. Genetic analysis in Bacillus subtilis. Methods Enzymol 204:305-320.
    • (1991) Methods Enzymol , vol.204 , pp. 305-320
    • Hoch, J.A.1
  • 24
    • 0029916568 scopus 로고    scopus 로고
    • Transcriptional analysis of bglPH expression in Bacillus subtilis: Evidence for two distinct pathways mediating carbon catabolite repression
    • Krüger, S., Gertz, S., Hecker, M. 1996. Transcriptional analysis of bglPH expression in Bacillus subtilis: evidence for two distinct pathways mediating carbon catabolite repression. J Bacteriol 178:2637-2644.
    • (1996) J Bacteriol , vol.178 , pp. 2637-2644
    • Krüger, S.1    Gertz, S.2    Hecker, M.3
  • 25
    • 0033814534 scopus 로고    scopus 로고
    • Characterization of the ccpA gene of Enterococcus faecalis: Identification of starvation-inducible proteins regulated by ccpA
    • Leboeuf, C., Leblanc, L., Auffray, Y., Hartke, A. 2000. Characterization of the ccpA gene of Enterococcus faecalis: identification of starvation-inducible proteins regulated by ccpA. J Bacteriol 182:5799-5806.
    • (2000) J Bacteriol , vol.182 , pp. 5799-5806
    • Leboeuf, C.1    Leblanc, L.2    Auffray, Y.3    Hartke, A.4
  • 26
    • 0034675992 scopus 로고    scopus 로고
    • Signal transduction between a membrane-bound transporter, PtsG, and a soluble transcription factor, Mlc, of Escherichia coli
    • Lee, S.J., Boos, W., Bouche, J.P., 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.
    • (2000) EMBO J , vol.19 , pp. 5353-5361
    • Lee, S.J.1    Boos, W.2    Bouche, J.P.3    Plumbridge, J.4
  • 27
    • 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.
    • (2002) J Bacteriol , vol.184 , pp. 4819-4828
    • Lindner, C.1    Hecker, M.2    Le Coq, D.3    Deutscher, J.4
  • 28
    • 0036065304 scopus 로고    scopus 로고
    • Control of the glycolytic gapA operon by the catabolite control protein a in Bacillus subtilis: A novel mechanism of CcpA-mediated regulation
    • Ludwig, H., Rebhan, N., Blencke, H.-M., Merzbacher, M., Stülke, J. 2002. Control of the glycolytic gapA operon by the catabolite control protein A in Bacillus subtilis: a novel mechanism of CcpA-mediated regulation. Mol Microbiol 45:543-553.
    • (2002) Mol Microbiol , vol.45 , pp. 543-553
    • Ludwig, H.1    Rebhan, N.2    Blencke, H.-M.3    Merzbacher, M.4    Stülke, J.5
  • 29
    • 0024523666 scopus 로고
    • Induction and metabolite regulation of levanase synthesis in Bacillus subtilis
    • Martin, I., Débarbouillé, M., Klier, A., Rapoport, G. 1989. Induction and metabolite regulation of levanase synthesis in Bacillus subtilis. J Bacteriol 171:1885-1892.
    • (1989) J Bacteriol , vol.171 , pp. 1885-1892
    • Martin, I.1    Débarbouillé, M.2    Klier, A.3    Rapoport, G.4
  • 30
    • 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.
    • (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
  • 31
    • 0032716772 scopus 로고    scopus 로고
    • The Q15H mutation enables Crh, a Bacillus subtilis HPr-like protein, to carry out some regulatory HPr functions, but does not make it an effective phosphocarrier for sugar transport
    • Martin-Verstraete, I., Galinier, A., Darbon, E., Quentin, Y., Charrier, V., Kilhoffer, M.-C., Haiech, J., Rapoport, G., Deutscher, J. 1999. The Q15H mutation enables Crh, a Bacillus subtilis HPr-like protein, to carry out some regulatory HPr functions, but does not make it an effective phosphocarrier for sugar transport. Microbiology 145:3195-3204.
    • (1999) Microbiology , vol.145 , pp. 3195-3204
    • Martin-Verstraete, I.1    Galinier, A.2    Darbon, E.3    Quentin, Y.4    Charrier, V.5    Kilhoffer, M.-C.6    Haiech, J.7    Rapoport, G.8    Deutscher, J.9
  • 33
    • 0031024403 scopus 로고    scopus 로고
    • Carbon-source regulation of virulence gene expression in Listeria monocytogenes
    • Milenbachs, A.A., Brown, D.P., Moors, M., Youngman, P. 1997. Carbon-source regulation of virulence gene expression in Listeria monocytogenes. Mol Microbiol 23:1075-1085.
    • (1997) Mol Microbiol , vol.23 , pp. 1075-1085
    • Milenbachs, A.A.1    Brown, D.P.2    Moors, M.3    Youngman, P.4
  • 34
    • 1242273731 scopus 로고    scopus 로고
    • Deregulation of Listeria monocytogenes virulence gene expression by two distinct and semi-independent pathways
    • Milenbachs Lukowiak, A., Mueller, K.J., Freitag, N.E., Youngman, P. 2004. Deregulation of Listeria monocytogenes virulence gene expression by two distinct and semi-independent pathways. Microbiology 150:321-333.
    • (2004) Microbiology , vol.150 , pp. 321-333
    • Milenbachs Lukowiak, A.1    Mueller, K.J.2    Freitag, N.E.3    Youngman, P.4
  • 35
    • 0035026054 scopus 로고    scopus 로고
    • Regulatory functions of serine-46-phosphorylated HPr in Lactococcus lactis
    • Monedero, V., Kuipers, O.P., Jamet, E., Deutscher, J. 2001. Regulatory functions of serine-46-phosphorylated HPr in Lactococcus lactis. J Bacteriol 183:3391-3398.
    • (2001) J Bacteriol , vol.183 , pp. 3391-3398
    • Monedero, V.1    Kuipers, O.P.2    Jamet, E.3    Deutscher, J.4
  • 38
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate: Carbohydrate phosphotransferase systems of bacteria
    • Postma, P.W., Lengeler, J.W., Jacobson, G.R. 1993. Phosphoenolpyruvate: carbohydrate phosphotransferase systems of bacteria. Microbiol Rev 57:543-594.
    • (1993) Microbiol Rev , vol.57 , pp. 543-594
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 40
    • 0026806524 scopus 로고
    • Functional interactions between proteins of the phosphoenolpyruvate:sugar phosphotransferase systems of Bacillus subtilis and Escherichia coli
    • Reizer, J., Sutrina, S.L., Wu, L.-F., Deutscher, J., Reddy, P., Saier, M.H. Jr. 1992. Functional interactions between proteins of the phosphoenolpyruvate:sugar phosphotransferase systems of Bacillus subtilis and Escherichia coli. J Biol Chem 267:9158-9169.
    • (1992) J Biol Chem , vol.267 , pp. 9158-9169
    • Reizer, J.1    Sutrina, S.L.2    Wu, L.-F.3    Deutscher, J.4    Reddy, P.5    Saier Jr., M.H.6
  • 41
    • 4544356004 scopus 로고    scopus 로고
    • Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P
    • Schumacher, M.A., Allen, G.S., Diel, M., Seidel, G., Hillen, W., Brennan, R.G. 2004. Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P. Cell 118:731-741.
    • (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
  • 42
    • 0028855910 scopus 로고
    • Differential activation of virulence gene expression by PrfA, the Listeria monocytogenes virulence regulator
    • Sheehan, B., Klarsfeld, A., Msadek, T., Cossart, P. 1995. Differential activation of virulence gene expression by PrfA, the Listeria monocytogenes virulence regulator. J Bacteriol 177:6469-6476.
    • (1995) J Bacteriol , vol.177 , pp. 6469-6476
    • Sheehan, B.1    Klarsfeld, A.2    Msadek, T.3    Cossart, P.4
  • 43
    • 0028354905 scopus 로고
    • Plasmids designed to alter the antibiotic resistance expressed by insertion mutations in Bacillus subtilis, through in vivo recombination
    • Steinmetz, M., Richter, R. 1994. Plasmids designed to alter the antibiotic resistance expressed by insertion mutations in Bacillus subtilis, through in vivo recombination. Gene 142:79-83.
    • (1994) Gene , vol.142 , pp. 79-83
    • Steinmetz, M.1    Richter, R.2
  • 44
    • 0031808469 scopus 로고    scopus 로고
    • PRD - A protein domain involved in PTS-dependent induction and carbon catabolite repression of catabolic operons in bacteria
    • Stülke, J., Arnaud, M., Rapoport, G., Martin-Verstraete, I. 1998. PRD - a protein domain involved in PTS-dependent induction and carbon catabolite repression of catabolic operons in bacteria. Mol Microbiol 28:865-874.
    • (1998) Mol Microbiol , vol.28 , pp. 865-874
    • Stülke, J.1    Arnaud, M.2    Rapoport, G.3    Martin-Verstraete, I.4
  • 45
    • 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.
    • (2000) EMBO J , vol.19 , pp. 5344-5352
    • Tanaka, Y.1    Kimata, K.2    Aiba, H.3
  • 46
    • 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.
    • (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
  • 47
    • 0028364815 scopus 로고
    • Regulation of the glucose: H+ symporter by metabolite-activated ATP-dependent phosphorylation of HPr in Lactobacillus brevis
    • Ye, J.-J., Neal, J.W., Cui, X., Reizer, J., Saier Jr, M.H. 1994. Regulation of the glucose:H+ symporter by metabolite-activated ATP-dependent phosphorylation of HPr in Lactobacillus brevis. J Bacteriol 176:3484-3492.
    • (1994) J Bacteriol , vol.176 , pp. 3484-3492
    • Ye, J.-J.1    Neal, J.W.2    Cui, X.3    Reizer, J.4    Saier Jr., M.H.5
  • 48
    • 30744457819 scopus 로고    scopus 로고
    • Interaction between the Yersinia tyrosine phosphatase YopH and its macrophage substrate Fyn binding protein, FYB
    • Yuan, M., Deleuil, F., Fällman, M. 2005. Interaction between the Yersinia tyrosine phosphatase YopH and its macrophage substrate Fyn binding protein, FYB. J Mol Biol Biotechnol 9:214-223.
    • (2005) J Mol Biol Biotechnol , vol.9 , pp. 214-223
    • Yuan, M.1    Deleuil, F.2    Fällman, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.