메뉴 건너뛰기




Volumn 9, Issue 3-4, 2006, Pages 125-131

Ser/Thr/Tyr protein phosphorylation in bacteria - For long time neglected, now well established

Author keywords

Bacteria; Protein kinases; Protein phosphatases; Protein phosphorylation

Indexed keywords

ABC TRANSPORTER; BACTERIAL ENZYME; ESCHERICHIA COLI PROTEIN; GLYCINE CLEAVAGE SYSTEM; ISOCITRATE DEHYDROGENASE; NUCLEOTIDE BINDING PROTEIN; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN SERINE THREONINE KINASE; PROTEIN SERINE THREONINE PHOSPHATASE; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE; UNCLASSIFIED DRUG;

EID: 30744464566     PISSN: 14641801     EISSN: None     Source Type: Journal    
DOI: 10.1159/000089641     Document Type: Conference Paper
Times cited : (128)

References (83)
  • 1
    • 0037470605 scopus 로고    scopus 로고
    • Crystal structure of HPr kinase/phosphatase from Mycoplasma pneumoniae
    • Allen, G.S., Steinhauer, K., Hillen, W., Stülke, J., Brennan, R.G. 2003. Crystal structure of HPr kinase/phosphatase from Mycoplasma pneumoniae. J Mol Biol 326:1203-1217.
    • (2003) J Mol Biol , vol.326 , pp. 1203-1217
    • Allen, G.S.1    Steinhauer, K.2    Hillen, W.3    Stülke, J.4    Brennan, R.G.5
  • 2
    • 7944222488 scopus 로고    scopus 로고
    • First structural glimpse at a bacterial Ser/Thr protein phosphatase
    • Alzari, P.M. 2004. First structural glimpse at a bacterial Ser/Thr protein phosphatase. Structure 12:1923-1924.
    • (2004) Structure , vol.12 , pp. 1923-1924
    • Alzari, P.M.1
  • 3
    • 0029559466 scopus 로고
    • Protein phosphatases
    • Barford, D. 1995. Protein phosphatases. Curr Opin Struct Biol 5:728-734.
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 728-734
    • Barford, D.1
  • 4
    • 0035930626 scopus 로고    scopus 로고
    • CpsB is a modulator of capsule-associated tyrosine kinase activity in Streptococcus pneumoniae
    • Bender, M.H., Yother, J. 2001. CpsB is a modulator of capsule-associated tyrosine kinase activity in Streptococcus pneumoniae. J Biol Chem 276:47966-47974.
    • (2001) J Biol Chem , vol.276 , pp. 47966-47974
    • Bender, M.H.1    Yother, J.2
  • 6
    • 0017407844 scopus 로고
    • The hormonal control of glycogen metabolism: The amino acid sequence at the phosphorylation site of protein phosphatase inhibitor-1
    • Cohen, P., Rylatt, D.B., Nimmo, G.A. 1977. The hormonal control of glycogen metabolism: the amino acid sequence at the phosphorylation site of protein phosphatase inhibitor-1. FEBS Lett 76:182-186.
    • (1977) FEBS Lett , vol.76 , pp. 182-186
    • Cohen, P.1    Rylatt, D.B.2    Nimmo, G.A.3
  • 7
    • 0035831155 scopus 로고    scopus 로고
    • Crystal structure of the bacterial cell division regulator MinD
    • Cordell, S.C., Lowe, J. 2001. Crystal structure of the bacterial cell division regulator MinD. FEBS Lett 492:160-165.
    • (2001) FEBS Lett , vol.492 , pp. 160-165
    • Cordell, S.C.1    Lowe, J.2
  • 8
    • 0003173225 scopus 로고
    • Crystalline muscle phosphorylase. II. Prosthetic group
    • Cori, G.T., Green, A.A. 1943. Crystalline muscle phosphorylase. II. Prosthetic group. J Biol Chem 151:31-38.
    • (1943) J Biol Chem , vol.151 , pp. 31-38
    • Cori, G.T.1    Green, A.A.2
  • 9
    • 0022774381 scopus 로고
    • Characterization of the phosphoproteins of Escherichia coli cells by electrophoretic analysis
    • Cortay, J.C., Rieul, C., Duclos, B., Cozzone, A.J. 1986. Characterization of the phosphoproteins of Escherichia coli cells by electrophoretic analysis. Eur J Biochem 159:227-237.
    • (1986) Eur J Biochem , vol.159 , pp. 227-237
    • Cortay, J.C.1    Rieul, C.2    Duclos, B.3    Cozzone, A.J.4
  • 10
    • 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
  • 11
    • 30744432855 scopus 로고    scopus 로고
    • Control of isocitrate dehydrogenase catalytic activity by protein phosphorylation in Escherichia coli
    • Cozzone, A.J., El-Mansi, M. 2005. Control of isocitrate dehydrogenase catalytic activity by protein phosphorylation in Escherichia coli. J Mol Microbiol Biotechnol 9:132-146.
    • (2005) J Mol Microbiol Biotechnol , vol.9 , pp. 132-146
    • Cozzone, A.J.1    El-Mansi, M.2
  • 12
    • 30744437442 scopus 로고
    • Isolation of phosphothreonine from bovine casein
    • de Verdier, C.-H. 1952. Isolation of phosphothreonine from bovine casein. Nature 170:804-805.
    • (1952) Nature , vol.170 , pp. 804-805
    • De Verdier, C.-H.1
  • 13
    • 0014409136 scopus 로고
    • Activation of skeletal muscle phosphorylase kinase by adenosine triphosphate and adenosine 3′,5′-monophosphate
    • DeLange, R.J., Kemp, R.G., Riley, W.D., Cooper, R.A., Krebs, E.G. 1968. Activation of skeletal muscle phosphorylase kinase by adenosine triphosphate and adenosine 3′,5′-monophosphate. J Biol Chem 243:2200-2208.
    • (1968) J Biol Chem , vol.243 , pp. 2200-2208
    • DeLange, R.J.1    Kemp, R.G.2    Riley, W.D.3    Cooper, R.A.4    Krebs, E.G.5
  • 15
    • 29144490206 scopus 로고    scopus 로고
    • P-Ser-HPr - A link between carbon metabolism and the virulence of certain pathogenic bacteria
    • epub ahead of print
    • Deutscher, J., Herro, R., Bourand, A., Mijakovic, I., Poncet, P. 2005. P-Ser-HPr - a link between carbon metabolism and the virulence of certain pathogenic bacteria. Biochim Biophys Acta [epub ahead of print].
    • (2005) Biochim Biophys Acta
    • Deutscher, J.1    Herro, R.2    Bourand, A.3    Mijakovic, I.4    Poncet, P.5
  • 16
    • 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
  • 17
    • 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, 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, M.H.2
  • 19
    • 0028788997 scopus 로고
    • Activation of cell-specific transcription by a serine phosphatase at the site of asymmetric division
    • Duncan, L., Alper, S., Arigoni, F., Losick, R., Stragier, P. 1995. Activation of cell-specific transcription by a serine phosphatase at the site of asymmetric division. Science 270:641-644.
    • (1995) Science , vol.270 , pp. 641-644
    • Duncan, L.1    Alper, S.2    Arigoni, F.3    Losick, R.4    Stragier, P.5
  • 20
    • 0033638454 scopus 로고    scopus 로고
    • The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms
    • Durocher, D., Taylor, I.A., Sarbassova, D., Haire, L.F., Westcott, S.L., Jackson, S.P., Smerdon, S.J., Yaffe, M.B. 2000. The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms. Mol Cell 6:1169-1182.
    • (2000) Mol Cell , vol.6 , pp. 1169-1182
    • Durocher, D.1    Taylor, I.A.2    Sarbassova, D.3    Haire, L.F.4    Westcott, S.L.5    Jackson, S.P.6    Smerdon, S.J.7    Yaffe, M.B.8
  • 23
    • 0000187410 scopus 로고
    • Conversion of phosphorylase b to phosphorylase a in muscle extracts
    • Fischer, E.H., Krebs, E.G. 1955. Conversion of phosphorylase b to phosphorylase a in muscle extracts. J Biol Chem 216:121-132.
    • (1955) J Biol Chem , vol.216 , pp. 121-132
    • Fischer, E.H.1    Krebs, E.G.2
  • 24
    • 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
  • 26
    • 0018397107 scopus 로고
    • Phosphorylation of isocitrate dehydrogenase of Escherichia coli
    • Garnak, M., Reeves, H.C. 1979. Phosphorylation of isocitrate dehydrogenase of Escherichia coli. Science 203:1111-1112.
    • (1979) Science , vol.203 , pp. 1111-1112
    • Garnak, M.1    Reeves, H.C.2
  • 27
    • 12144278799 scopus 로고    scopus 로고
    • Biochemical characterization of phosphoryl transfer involving HPr of the phosphoenolpyruvate-dependent phosphotransferase system in Treponema denticola, an organism that lacks PTS permeases
    • Gonzalez, C.F., Stonestrom, A.J., Lorca, G.L., Saier, M.H., Jr. 2005. Biochemical characterization of phosphoryl transfer involving HPr of the phosphoenolpyruvate-dependent phosphotransferase system in Treponema denticola, an organism that lacks PTS permeases. Biochemistry 44:598-608.
    • (2005) Biochemistry , vol.44 , pp. 598-608
    • Gonzalez, C.F.1    Stonestrom, A.J.2    Lorca, G.L.3    Saier Jr., M.H.4
  • 28
    • 0141574316 scopus 로고    scopus 로고
    • Autophosphorylation of the Escherichia coli protein kinase Wzc regulates tyrosine phosphorylation of Ugd, a UDP-glucose dehydrogenase
    • Grangeasse, C., Obadia, B., Mijakovic, I., Deutscher, J., Cozzone, A.J., Doublet, P. 2003. Autophosphorylation of the Escherichia coli protein kinase Wzc regulates tyrosine phosphorylation of Ugd, a UDP-glucose dehydrogenase. J Biol Chem 278:39323-39329.
    • (2003) J Biol Chem , vol.278 , pp. 39323-39329
    • Grangeasse, C.1    Obadia, B.2    Mijakovic, I.3    Deutscher, J.4    Cozzone, A.J.5    Doublet, P.6
  • 30
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • Hanks, S.K., Quinn, A.M., Hunter, T. 1988. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 241:42-52.
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 31
    • 0035901493 scopus 로고    scopus 로고
    • Structural and functional studies of MinD ATPase: Implications for the molecular recognition of the bacterial cell division apparatus
    • Hayashi, I., Oyama, T., Morikawa, K. 2001. Structural and functional studies of MinD ATPase: implications for the molecular recognition of the bacterial cell division apparatus. EMBO J 20:1819-1828.
    • (2001) EMBO J , vol.20 , pp. 1819-1828
    • Hayashi, I.1    Oyama, T.2    Morikawa, K.3
  • 32
  • 33
    • 0029360452 scopus 로고
    • The FHA domain: A putative nuclear signalling domain found in protein kinases and transcription factors
    • Hofmann, K., Bucher, P. 1995. The FHA domain: a putative nuclear signalling domain found in protein kinases and transcription factors. Trends Biochem Sci 20:347-349.
    • (1995) Trends Biochem Sci , vol.20 , pp. 347-349
    • Hofmann, K.1    Bucher, P.2
  • 34
    • 0036034303 scopus 로고    scopus 로고
    • Phylogeny of phosphoryl transfer proteins of the phosphoenolpyruvate- dependent sugar transporting phosphotransferase system
    • Hu, K.-Y., Saier, M.H., Jr. 2002. Phylogeny of phosphoryl transfer proteins of the phosphoenolpyruvate-dependent sugar transporting phosphotransferase system. Res Microbiol 153:405-415.
    • (2002) Res Microbiol , vol.153 , pp. 405-415
    • Hu, K.-Y.1    Saier Jr., M.H.2
  • 35
    • 0000109995 scopus 로고
    • Transforming gene product of Rous sarcoma virus phosphorylates tyrosine
    • USA
    • Hunter, T., Sefton, B.M. 1980. Transforming gene product of Rous sarcoma virus phosphorylates tyrosine. Proc Natl Acad Sci USA 77:1311-1315.
    • (1980) Proc Natl Acad Sci , vol.77 , pp. 1311-1315
    • Hunter, T.1    Sefton, B.M.2
  • 36
    • 0037106478 scopus 로고    scopus 로고
    • PrpE, a PPP protein phosphatase from Bacillus subtilis with unusual substrate specificity
    • Iwanicki, A., Herman-Antosiewicz, A., Pierechod, M., Seror, S.J., Obuchowski, M. 2002. PrpE, a PPP protein phosphatase from Bacillus subtilis with unusual substrate specificity. Biochem J 366:929-936.
    • (2002) Biochem J , vol.366 , pp. 929-936
    • Iwanicki, A.1    Herman-Antosiewicz, A.2    Pierechod, M.3    Seror, S.J.4    Obuchowski, M.5
  • 37
    • 0037005989 scopus 로고    scopus 로고
    • Protein kinases and protein phosphatases in prokaryotes: A genomic perspective
    • Kennelly, P.J. 2002. Protein kinases and protein phosphatases in prokaryotes: a genomic perspective. FEMS Microbiol Lett 206:1-8.
    • (2002) FEMS Microbiol Lett , vol.206 , pp. 1-8
    • Kennelly, P.J.1
  • 38
    • 13244291292 scopus 로고    scopus 로고
    • Crystal structure of a complex between the catalytic and regulatory (RIα) subunits of PKA
    • Kim, C., Xuong, N.H., Taylor, S.S. 2005. Crystal structure of a complex between the catalytic and regulatory (RIα) subunits of PKA. Science 307:690-696.
    • (2005) Science , vol.307 , pp. 690-696
    • Kim, C.1    Xuong, N.H.2    Taylor, S.S.3
  • 39
    • 30744470097 scopus 로고    scopus 로고
    • A new tyrosine phosphorylation mechanism involved in signal transduction in Bacillus subtilis
    • Kirstein, J., Turgay, K. 2005. A new tyrosine phosphorylation mechanism involved in signal transduction in Bacillus subtilis. J Mol Microbiol Biotechnol 9:182-188.
    • (2005) J Mol Microbiol Biotechnol , vol.9 , pp. 182-188
    • Kirstein, J.1    Turgay, K.2
  • 40
    • 27144440950 scopus 로고    scopus 로고
    • A tyrosine kinase and its activator control the activity of the CtsR heat shock repressor in B. subtilis
    • Kirstein, J., Zühlke, D., Gerth, U., Turgay, K., Hecker, M. 2005. A tyrosine kinase and its activator control the activity of the CtsR heat shock repressor in B. subtilis. EMBO J 24:3435-3445.
    • (2005) EMBO J , vol.24 , pp. 3435-3445
    • Kirstein, J.1    Zühlke, D.2    Gerth, U.3    Turgay, K.4    Hecker, M.5
  • 41
    • 0037384743 scopus 로고    scopus 로고
    • Phosphorylation-mediated regulation of heat shock response in Escherichia coli
    • Klein, G., Dartigalongue, C., Raina, S. 2003. Phosphorylation-mediated regulation of heat shock response in Escherichia coli. Mol Microbiol 48:269-285.
    • (2003) Mol Microbiol , vol.48 , pp. 269-285
    • Klein, G.1    Dartigalongue, C.2    Raina, S.3
  • 42
  • 43
    • 0026326821 scopus 로고
    • Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton, D.R., Zheng, J.H., Ten Eyck, L.F., Xuong, N.H., Taylor, S.S., Sowadski, J.M. 1991b. Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253:414-420.
    • (1991) Science , vol.253 , pp. 414-420
    • Knighton, D.R.1    Zheng, J.H.2    Ten Eyck, L.F.3    Xuong, N.H.4    Taylor, S.S.5    Sowadski, J.M.6
  • 45
    • 0022392412 scopus 로고
    • A single gene codes for the kinase and phosphatase which regulate isocitrate dehydrogenase
    • LaPorte, D.C., Chung, T. 1985. A single gene codes for the kinase and phosphatase which regulate isocitrate dehydrogenase. J Biol Chem 260:15291-15297.
    • (1985) J Biol Chem , vol.260 , pp. 15291-15297
    • LaPorte, D.C.1    Chung, T.2
  • 46
    • 0000685288 scopus 로고
    • Serinephosphoric acid obtained on hydrolysis of vitellinic acid
    • Lipmann, F.A., Levene, P.A. 1932. Serinephosphoric acid obtained on hydrolysis of vitellinic acid. J Biol Chem 98:109-114.
    • (1932) J Biol Chem , vol.98 , pp. 109-114
    • Lipmann, F.A.1    Levene, P.A.2
  • 47
    • 0018574976 scopus 로고
    • Analysis of the protein-kinase activity of Escherichia coli cells
    • Manai, M., Cozzone, A.J. 1979. Analysis of the protein-kinase activity of Escherichia coli cells. Biochem Biophys Res Commun 91:819-826.
    • (1979) Biochem Biophys Res Commun , vol.91 , pp. 819-826
    • Manai, M.1    Cozzone, A.J.2
  • 48
    • 0037133589 scopus 로고    scopus 로고
    • Structure of the full-length HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 Å resolution: Mimicking the product/substrate of the phospho transfer reactions
    • USA
    • Marquez, J.A., Hasenbein, S., Koch, B., Fieulaine, S., Nessler, S., Russell, R.B., Hengstenberg, W., Scheffzek, K. 2002. Structure of the full-length HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 Å resolution: mimicking the product/substrate of the phospho transfer reactions. Proc Natl Acad Sci USA 99:3458-3463.
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 3458-3463
    • Marquez, J.A.1    Hasenbein, S.2    Koch, B.3    Fieulaine, S.4    Nessler, S.5    Russell, R.B.6    Hengstenberg, W.7    Scheffzek, K.8
  • 49
    • 0027980597 scopus 로고
    • Phosphorylation of the AfsR protein involved in secondary metabolism in Streptomyces species by a eukaryotic-type protein kinase
    • Matsumoto, A., Hong, S.K., Ishizuka, H., Horinouchi, S., Beppu, T. 1994. Phosphorylation of the AfsR protein involved in secondary metabolism in Streptomyces species by a eukaryotic-type protein kinase. Gene 146:47-56.
    • (1994) Gene , vol.146 , pp. 47-56
    • Matsumoto, A.1    Hong, S.K.2    Ishizuka, H.3    Horinouchi, S.4    Beppu, T.5
  • 54
    • 2342467904 scopus 로고    scopus 로고
    • Two FHA domains on an ABC transporter, Rv1747, mediate its phosphorylation by PknF, a Ser/Thr protein kinase from Mycobacterium tuberculosis
    • Molle, V., Soulat, D., Jault, J.M., Grangeasse, C., Cozzone, A.J., Prost, J.F. 2004. Two FHA domains on an ABC transporter, Rv1747, mediate its phosphorylation by PknF, a Ser/Thr protein kinase from Mycobacterium tuberculosis. FEMS Microbiol Lett 234:215-223.
    • (2004) FEMS Microbiol Lett , vol.234 , pp. 215-223
    • Molle, V.1    Soulat, D.2    Jault, J.M.3    Grangeasse, C.4    Cozzone, A.J.5    Prost, J.F.6
  • 55
    • 0025790172 scopus 로고
    • A gene encoding a protein serine/threonine kinase is required for normal development of M. xanthus, a gram-negative bacterium
    • Munoz-Dorado, J., Inouye, S., Inouye, M. 1991. A gene encoding a protein serine/threonine kinase is required for normal development of M. xanthus, a gram-negative bacterium. Cell 67:995-1006.
    • (1991) Cell , vol.67 , pp. 995-1006
    • Munoz-Dorado, J.1    Inouye, S.2    Inouye, M.3
  • 56
    • 0028989905 scopus 로고
    • Site of phosphorylation of SpoIIAA, the anti-anti-sigma factor for sporulation-specific sigma F of Bacillus subtilis
    • Najafi, S.M., Willis, A.C., Yudkin, M.D. 1995. Site of phosphorylation of SpoIIAA, the anti-anti-sigma factor for sporulation-specific sigma F of Bacillus subtilis. J Bacteriol 177:2912-2913.
    • (1995) J Bacteriol , vol.177 , pp. 2912-2913
    • Najafi, S.M.1    Willis, A.C.2    Yudkin, M.D.3
  • 57
    • 30744453516 scopus 로고    scopus 로고
    • Factors that modulate the Pkn4 kinase cascade in Myxococcus xanthus
    • Nariya, H., Inouye, S. 2005. Factors that modulate the Pkn4 kinase cascade in Myxococcus xanthus. J Mol Microbiol Biotechnol 9:147-153.
    • (2005) J Mol Microbiol Biotechnol , vol.9 , pp. 147-153
    • Nariya, H.1    Inouye, S.2
  • 58
    • 0017893010 scopus 로고
    • The regulation of glycogen metabolism. Phosphorylation of inhibitor-1 from rabbit skeletal muscle, and its interaction with protein phosphatases-III and -II
    • Nimmo, G.A., Cohen, P. 1978. The regulation of glycogen metabolism. Phosphorylation of inhibitor-1 from rabbit skeletal muscle, and its interaction with protein phosphatases-III and -II. Eur J Biochem 15:353-365.
    • (1978) Eur J Biochem , vol.15 , pp. 353-365
    • Nimmo, G.A.1    Cohen, P.2
  • 60
    • 0037969625 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis
    • Ortiz-Lombardia, M., Pompeo, F., Boitel, B., Alzari, P.M. 2003. Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis. J Biol Chem 278:13094-13100.
    • (2003) J Biol Chem , vol.278 , pp. 13094-13100
    • Ortiz-Lombardia, M.1    Pompeo, F.2    Boitel, B.3    Alzari, P.M.4
  • 61
    • 0036966368 scopus 로고    scopus 로고
    • Bacterial FHA domains: Neglected players in the phospho-threonine signalling game?
    • Pallen, M., Chaudhuri, R., Khan, A. 2002. Bacterial FHA domains: neglected players in the phospho-threonine signalling game? Trends Microbiol 10:556-563.
    • (2002) Trends Microbiol , vol.10 , pp. 556-563
    • Pallen, M.1    Chaudhuri, R.2    Khan, A.3
  • 62
    • 0026484261 scopus 로고
    • SH2 and SH3 domains: From structure to function
    • Pawson, T., Gish, G.D. 1992. SH2 and SH3 domains: from structure to function. Cell 71:359-362.
    • (1992) Cell , vol.71 , pp. 359-362
    • Pawson, T.1    Gish, G.D.2
  • 63
    • 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
  • 64
    • 7944221188 scopus 로고    scopus 로고
    • An alternate conformation and a third metal in PstP/Ppp, the M. tuberculosis PP2C-family Ser/Thr protein phosphatase
    • Pullen, K.E., Ng, H.L., Sung, P.Y., Good, M.C., Smith, S.M., Alber, T. 2004. An alternate conformation and a third metal in PstP/Ppp, the M. tuberculosis PP2C-family Ser/Thr protein phosphatase. Structure 12:1947-1954.
    • (2004) Structure , vol.12 , pp. 1947-1954
    • Pullen, K.E.1    Ng, H.L.2    Sung, P.Y.3    Good, M.C.4    Smith, S.M.5    Alber, T.6
  • 65
    • 30744436337 scopus 로고
    • Identification of a new form of bound phosphoserine in Escherichia coli
    • Rafter, G.W. 1964. Identification of a new form of bound phosphoserine in Escherichia coli. J Biol Chem 239:1044-1047.
    • (1964) J Biol Chem , vol.239 , pp. 1044-1047
    • Rafter, G.W.1
  • 68
    • 0020553970 scopus 로고
    • Mechanism of inducer expulsion in Streptococcus pyogenes: A two-step process activated by ATP
    • Reizer, J., Novotny, M.J., Panos, C., Saier, M.H., 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
  • 70
    • 18144406818 scopus 로고    scopus 로고
    • Structural and functional analysis of the C-terminal STAS (sulfate transporter and anti-sigma antagonist) domain of the Arabidopsis thaliana sulfate transporter SULTR1.2
    • Rouached, H., Berthomieu, P., El Kassis, E., Cathala, N., Catherinot, V., Labesse, G., Davidian, J.C., Fourcroy, P. 2005. Structural and functional analysis of the C-terminal STAS (sulfate transporter and anti-sigma antagonist) domain of the Arabidopsis thaliana sulfate transporter SULTR1.2. J Biol Chem 280:15976-15983.
    • (2005) J Biol Chem , vol.280 , pp. 15976-15983
    • Rouached, H.1    Berthomieu, P.2    El Kassis, E.3    Cathala, N.4    Catherinot, V.5    Labesse, G.6    Davidian, J.C.7    Fourcroy, P.8
  • 72
    • 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
  • 73
    • 0018743506 scopus 로고
    • Product of in vitro translation of the Rous sarcoma virus src gene has protein kinase activity
    • Sefton, B.M., Hunter, T., Beemon, K. 1979. Product of in vitro translation of the Rous sarcoma virus src gene has protein kinase activity. J Virol 30:311-318.
    • (1979) J Virol , vol.30 , pp. 311-318
    • Sefton, B.M.1    Hunter, T.2    Beemon, K.3
  • 74
    • 0033538077 scopus 로고    scopus 로고
    • Cyanobacterial PPP family protein phosphatases possess multifunctional capabilities and are resistant to microcystin-LR
    • Shi, L., Carmichael, W.W., Kennelly, P.J. 1999. Cyanobacterial PPP family protein phosphatases possess multifunctional capabilities and are resistant to microcystin-LR. J Biol Chem 274:10039-10046.
    • (1999) J Biol Chem , vol.274 , pp. 10039-10046
    • Shi, L.1    Carmichael, W.W.2    Kennelly, P.J.3
  • 75
    • 16844380912 scopus 로고    scopus 로고
    • Bioinformatic analyses of bacterial HPr kinase homologues
    • Stonestrom, A., Gonzalez, C., Saier, M.H., Jr. 2005. Bioinformatic analyses of bacterial HPr kinase homologues. Res Microbiol 156:443-451.
    • (2005) Res Microbiol , vol.156 , pp. 443-451
    • Stonestrom, A.1    Gonzalez, C.2    Saier Jr., M.H.3
  • 76
    • 0001268037 scopus 로고
    • Inactivation and activation of liver phosphorylase
    • Sutherland, E.W., Wosilait, W.D. 1955. Inactivation and activation of liver phosphorylase. Nature 175:169-170.
    • (1955) Nature , vol.175 , pp. 169-170
    • Sutherland, E.W.1    Wosilait, W.D.2
  • 77
    • 20744445530 scopus 로고    scopus 로고
    • Proteomic identification of Mycobacterium tuberculosis protein kinase substrates: PknB recruits GarA, a FHA domain-containing protein, through activation loop-mediated interactions
    • Villarino, A., Duran, R., Wehenkel, A., Fernandez, P., England, P., Brodin, P., Cole, S.T., Zimny-Arndt, U., Jungblut, P.R., Cervenansky, C., Alzari, P.M. 2005. Proteomic identification of Mycobacterium tuberculosis protein kinase substrates: PknB recruits GarA, a FHA domain-containing protein, through activation loop-mediated interactions. J Mol Biol 350:953-963.
    • (2005) J Mol Biol , vol.350 , pp. 953-963
    • Villarino, A.1    Duran, R.2    Wehenkel, A.3    Fernandez, P.4    England, P.5    Brodin, P.6    Cole, S.T.7    Zimny-Arndt, U.8    Jungblut, P.R.9    Cervenansky, C.10    Alzari, P.M.11
  • 78
    • 0018265453 scopus 로고
    • Evidence for protein kinase activities in the prokaryote Salmonella typhimurium
    • Wang, J.Y., Koshland, D.E. 1978. Evidence for protein kinase activities in the prokaryote Salmonella typhimurium. J Biol Chem 253:7605-7608.
    • (1978) J Biol Chem , vol.253 , pp. 7605-7608
    • Wang, J.Y.1    Koshland, D.E.2
  • 79
    • 0033539643 scopus 로고    scopus 로고
    • A novel bacterial tyrosine kinase essential for cell division and differentiation
    • USA
    • Wu, J., Ohta, N., Zhao, J.L., Newton, A. 1999. A novel bacterial tyrosine kinase essential for cell division and differentiation. Proc Natl Acad Sci USA 96:13068-13073.
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 13068-13073
    • Wu, J.1    Ohta, N.2    Zhao, J.L.3    Newton, A.4
  • 80
    • 0037337317 scopus 로고    scopus 로고
    • Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases
    • Young, T.A., Delagoutte, B., Endrizzi, J.A., Falick, A.M., Alber, T. 2003. Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases. Nat Struct Biol 10:168-174.
    • (2003) Nat Struct Biol , vol.10 , pp. 168-174
    • Young, T.A.1    Delagoutte, B.2    Endrizzi, J.A.3    Falick, A.M.4    Alber, T.5
  • 81
    • 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 Microbiol Biotechnol 9:214-223.
    • (2005) J Mol Microbiol Biotechnol , vol.9 , pp. 214-223
    • Yuan, M.1    Deleuil, F.2    Fällman, M.3
  • 82
    • 30744463252 scopus 로고    scopus 로고
    • Protein phosphorylation on Ser, Thr and Tyr residues in cyanobacteria
    • Zhang, C.-C., Jang, J., Sakr, S., Wang, L. 2005. Protein phosphorylation on Ser, Thr and Tyr residues in cyanobacteria. J Mol Microbiol Biotechnol 9:154-166.
    • (2005) J Mol Microbiol Biotechnol , vol.9 , pp. 154-166
    • Zhang, C.-C.1    Jang, J.2    Sakr, S.3    Wang, L.4
  • 83
    • 0016760411 scopus 로고
    • In vivo and in vitro phosphorylation of DNA-dependent RNA polymerase of Escherichia coli by bacteriophage-T7-induced protein kinase
    • USA
    • Zillig, W., Fujiki, H., Blum, W., Janekovic, D., Schweiger, M., Rahmsdorf, H.-J., Ponta, H., Hirsch-Kauffmann, M. 1975. In vivo and in vitro phosphorylation of DNA-dependent RNA polymerase of Escherichia coli by bacteriophage-T7-induced protein kinase. Proc Natl Acad Sci USA 72:2506-2510.
    • (1975) Proc Natl Acad Sci , vol.72 , pp. 2506-2510
    • Zillig, W.1    Fujiki, H.2    Blum, W.3    Janekovic, D.4    Schweiger, M.5    Rahmsdorf, H.-J.6    Ponta, H.7    Hirsch-Kauffmann, M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.