메뉴 건너뛰기




Volumn 78, Issue 1, 2010, Pages 184-192

The stability of cytadherence proteins in Mycoplasma pneumoniae requires activity of the protein kinase PrkC

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; BACTERIAL PROTEIN; CYTADHERENCE PROTEIN; MEMBRANE PROTEIN; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN KINASE C; UNCLASSIFIED DRUG;

EID: 73449134487     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.00958-09     Document Type: Article
Times cited : (33)

References (35)
  • 2
    • 64049118984 scopus 로고    scopus 로고
    • Absalon, C., M. Obuchowski, E. Madec, D. Delattre, I. B. Holland, and S. J. Séror. 2009. CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis. Microbiology 155:932-943.
    • Absalon, C., M. Obuchowski, E. Madec, D. Delattre, I. B. Holland, and S. J. Séror. 2009. CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis. Microbiology 155:932-943.
  • 3
    • 0037470605 scopus 로고    scopus 로고
    • Crystal structure of HPr kinase/phosphatase from Mycoplasma pneumonia
    • Allen, G. S., K. Steinhauer, W. Hillen, J. Stülke, and R. G. Brennan. 2003. Crystal structure of HPr kinase/phosphatase from Mycoplasma pneumonia. 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
  • 4
    • 53749101273 scopus 로고    scopus 로고
    • Epidemiology, clinical manifestations, pathogenesis and laboratory detection of Mycoplasma pneumoniae infections
    • Atkinson, T. P., M. F. Balish, and K. B. Waites. 2008. Epidemiology, clinical manifestations, pathogenesis and laboratory detection of Mycoplasma pneumoniae infections. FEMS Microbiol. Rev. 32:956-973.
    • (2008) FEMS Microbiol. Rev , vol.32 , pp. 956-973
    • Atkinson, T.P.1    Balish, M.F.2    Waites, K.B.3
  • 5
    • 33748770937 scopus 로고    scopus 로고
    • Mycoplasmas: A distinct cytoskeleton for wall-less bacteria
    • Balish, M. F., and D. C. Krause. 2006. Mycoplasmas: a distinct cytoskeleton for wall-less bacteria. J. Mol. Microbiol. Biotechnol. 11:244-255.
    • (2006) J. Mol. Microbiol. Biotechnol , vol.11 , pp. 244-255
    • Balish, M.F.1    Krause, D.C.2
  • 6
    • 0346887117 scopus 로고    scopus 로고
    • Deletion analysis identifies key functional domains of the cytadherence- associated protein HMW2 of Mycoplasma pneumoniae
    • Balish, M. F., S. M. Ross, M. Fisseha, and D. C. Krause. 2003. Deletion analysis identifies key functional domains of the cytadherence- associated protein HMW2 of Mycoplasma pneumoniae. Mol. Microbiol. 50:1507-1516.
    • (2003) Mol. Microbiol , vol.50 , pp. 1507-1516
    • Balish, M.F.1    Ross, S.M.2    Fisseha, M.3    Krause, D.C.4
  • 7
    • 57449119872 scopus 로고    scopus 로고
    • The gene mpn310 (hmw2) from Mycoplasma pneumoniae encodes two proteins, HMW2 and HMW2-s, which differ in size but use the same reading frame
    • Boonmee, A., T. Ruppert, and R. Herrmann. 2009. The gene mpn310 (hmw2) from Mycoplasma pneumoniae encodes two proteins, HMW2 and HMW2-s, which differ in size but use the same reading frame. FEMS Microbiol. Lett. 290:174-181.
    • (2009) FEMS Microbiol. Lett , vol.290 , pp. 174-181
    • Boonmee, A.1    Ruppert, T.2    Herrmann, R.3
  • 9
    • 0028109456 scopus 로고
    • Phosphorylation of cytadherence-accessory proteins in Mycoplasma pneumoniae
    • Dirksen, L. B., K. A. Krebes, and D. C. Krause. 1994. Phosphorylation of cytadherence-accessory proteins in Mycoplasma pneumoniae. J. Bacteriol. 176:7499-7505.
    • (1994) J. Bacteriol , vol.176 , pp. 7499-7505
    • Dirksen, L.B.1    Krebes, K.A.2    Krause, D.C.3
  • 10
    • 34648857991 scopus 로고    scopus 로고
    • Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis
    • Eymann, C., D. Becher, J. Bernhardt, K. Gronau, A. Klutzny, and M. Hecker. 2007. Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis. Proteomics 7:3509-3526.
    • (2007) Proteomics , vol.7 , pp. 3509-3526
    • Eymann, C.1    Becher, D.2    Bernhardt, J.3    Gronau, K.4    Klutzny, A.5    Hecker, M.6
  • 11
    • 41049112960 scopus 로고    scopus 로고
    • The prpZ gene cluster encoding eukaryotic-type Ser/Thr protein kinases and phosphatases is repressed by oxidative stress and involved in Salmonella enterica serovar Typhi survival in human macrophages
    • Faucher, S. P., C. Viau, P. P. Gros, F. Daigle, and H. Le Moual. 2008. The prpZ gene cluster encoding eukaryotic-type Ser/Thr protein kinases and phosphatases is repressed by oxidative stress and involved in Salmonella enterica serovar Typhi survival in human macrophages. FEMS Microbiol. Lett. 281:160-166.
    • (2008) FEMS Microbiol. Lett , vol.281 , pp. 160-166
    • Faucher, S.P.1    Viau, C.2    Gros, P.P.3    Daigle, F.4    Le Moual, H.5
  • 14
    • 47549110972 scopus 로고    scopus 로고
    • Carbon catabolite repression in bacteria: Many ways to make the most out of nutrients
    • Görke, B., and J. Stülke. 2008. Carbon catabolite repression in bacteria: many ways to make the most out of nutrients. Nat. Rev. Microbiol. 6:613-624.
    • (2008) Nat. Rev. Microbiol , vol.6 , pp. 613-624
    • Görke, B.1    Stülke, J.2
  • 15
    • 0034738929 scopus 로고    scopus 로고
    • Bacterial genomics. Pump up the versatility
    • Greenberg, E. P. 2000. Bacterial genomics. Pump up the versatility. Nature 406:947-948.
    • (2000) Nature , vol.406 , pp. 947-948
    • Greenberg, E.P.1
  • 16
    • 20444407262 scopus 로고    scopus 로고
    • Dual phosphorylation of Mycoplasma pneumoniae HPr by Enzyme I and HPr kinase suggests an extended phosphoryl group susceptibility of HPr
    • Halbedel, S., and J. Stülke. 2005. Dual phosphorylation of Mycoplasma pneumoniae HPr by Enzyme I and HPr kinase suggests an extended phosphoryl group susceptibility of HPr. FEMS Microbiol. Lett. 247:193-198.
    • (2005) FEMS Microbiol. Lett , vol.247 , pp. 193-198
    • Halbedel, S.1    Stülke, J.2
  • 17
    • 9244229014 scopus 로고    scopus 로고
    • In vivo activity of enzymatic and regulatory components of the phosphoenolpyruvate:sugar phosphotransferase system in Mycoplasma pneumoniae
    • Halbedel, S., C. Hames, and J. Stülke. 2004. In vivo activity of enzymatic and regulatory components of the phosphoenolpyruvate:sugar phosphotransferase system in Mycoplasma pneumoniae. J. Bacteriol. 186:7936-7943.
    • (2004) J. Bacteriol , vol.186 , pp. 7936-7943
    • Halbedel, S.1    Hames, C.2    Stülke, J.3
  • 18
    • 33748755047 scopus 로고    scopus 로고
    • Regulatory protein phosphorylation in Mycoplasma pneumoniae: A PP2C-type phosphatase serves to dephosphorylate HPr(Ser-P)
    • Halbedel, S., J. Busse, S. R. Schmidl, and J. Stülke. 2006. Regulatory protein phosphorylation in Mycoplasma pneumoniae: a PP2C-type phosphatase serves to dephosphorylate HPr(Ser-P). J. Biol. Chem. 281:26253-26259.
    • (2006) J. Biol. Chem , vol.281 , pp. 26253-26259
    • Halbedel, S.1    Busse, J.2    Schmidl, S.R.3    Stülke, J.4
  • 19
    • 44349119834 scopus 로고    scopus 로고
    • The acidic, glutamine-rich Mpn474 protein of Mycoplasma pneumoniae is surface exposed and covers the complete cell
    • Hegermann, J., S. Halbedel, R. Dumke, J. Regula, R. R. Gaboulline, F. Mayer, J. Stülke, and R. Herrmann. 2008. The acidic, glutamine-rich Mpn474 protein of Mycoplasma pneumoniae is surface exposed and covers the complete cell. Microbiology 154:1185-1192.
    • (2008) Microbiology , vol.154 , pp. 1185-1192
    • Hegermann, J.1    Halbedel, S.2    Dumke, R.3    Regula, J.4    Gaboulline, R.R.5    Mayer, F.6    Stülke, J.7    Herrmann, R.8
  • 20
    • 51149113074 scopus 로고    scopus 로고
    • Phosphoproteomics in bacteria: Towards a systemic understanding of bacterial phosphorylation networks
    • Jers, C., B. Soufi, C. Grangeasse, J. Deutscher, and I. Mijakovic. 2008. Phosphoproteomics in bacteria: towards a systemic understanding of bacterial phosphorylation networks. Exp. Rev. Proteomics 5:619-627.
    • (2008) Exp. Rev. Proteomics , vol.5 , pp. 619-627
    • Jers, C.1    Soufi, B.2    Grangeasse, C.3    Deutscher, J.4    Mijakovic, I.5
  • 21
    • 33645054791 scopus 로고    scopus 로고
    • Identification and biochemical characterization of a eukaryotic-type serine/ threonine kinase and its cognate phosphatase in Streptococcus pyogenes: Their biological functions and substrate identification
    • Jin, H., and V. Pancholi. 2006. Identification and biochemical characterization of a eukaryotic-type serine/ threonine kinase and its cognate phosphatase in Streptococcus pyogenes: their biological functions and substrate identification. J. Mol. Biol. 357:1351-1372.
    • (2006) J. Mol. Biol , vol.357 , pp. 1351-1372
    • Jin, H.1    Pancholi, V.2
  • 22
    • 0027310848 scopus 로고
    • The effects of phosphorylation on the structure and function of proteins
    • Johnson, L. N., and D. Barford. 1993. The effects of phosphorylation on the structure and function of proteins. Annu. Rev. Biophys. Biomol. Struct. 22:199-232.
    • (1993) Annu. Rev. Biophys. Biomol. Struct , vol.22 , pp. 199-232
    • Johnson, L.N.1    Barford, D.2
  • 23
    • 33845980239 scopus 로고    scopus 로고
    • Protein P200 is dispensable for Mycoplasma pneumoniae hemadsorption but not gliding motility or colonization of differentiated bronchial epithelium
    • Jordan, J. L., H. Y. Chang, M. F. Balish, L. S. Holt, S. R. Bose, B. M. Hasselbring, R. H. Waldo III, T. M. Krunkosky, and D. C. Krause. 2007. Protein P200 is dispensable for Mycoplasma pneumoniae hemadsorption but not gliding motility or colonization of differentiated bronchial epithelium. Infect. Immun. 75:518-522.
    • (2007) Infect. Immun , vol.75 , pp. 518-522
    • Jordan, J.L.1    Chang, H.Y.2    Balish, M.F.3    Holt, L.S.4    Bose, S.R.5    Hasselbring, B.M.6    Waldo III, R.H.7    Krunkosky, T.M.8    Krause, D.C.9
  • 24
    • 0029127556 scopus 로고
    • Phosphorylation of Mycoplasma pneumoniae cytadherence-accessory proteins in cell extracts
    • Krebes, K. A., L. B. Dirksen, and D. C. Krause. 1995. Phosphorylation of Mycoplasma pneumoniae cytadherence-accessory proteins in cell extracts. J. Bacteriol. 177:4571-4574.
    • (1995) J. Bacteriol , vol.177 , pp. 4571-4574
    • Krebes, K.A.1    Dirksen, L.B.2    Krause, D.C.3
  • 25
    • 33847675357 scopus 로고    scopus 로고
    • A eukaryotic-type Ser/Thr kinase in Enterococcus faecalis mediates antimicrobial resistance and intestinal persistence
    • Kristich, C. J., C. L. Wells, and G. M. Dunny. 2007. A eukaryotic-type Ser/Thr kinase in Enterococcus faecalis mediates antimicrobial resistance and intestinal persistence. Proc. Natl. Acad. Sci. U. S. A. 104:3508-3513.
    • (2007) Proc. Natl. Acad. Sci. U. S. A , vol.104 , pp. 3508-3513
    • Kristich, C.J.1    Wells, C.L.2    Dunny, G.M.3
  • 27
    • 1642480263 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae HPr kinase/phosphorylase: Assigning functional roles to the Ploop and the HPrK/P signature sequence motif
    • Merzbacher, M., C. Detsch, W. Hillen, and J. Stülke. 2004. Mycoplasma pneumoniae HPr kinase/phosphorylase: assigning functional roles to the Ploop and the HPrK/P signature sequence motif. Eur. J. Biochem. 271:367-374.
    • (2004) Eur. J. Biochem , vol.271 , pp. 367-374
    • Merzbacher, M.1    Detsch, C.2    Hillen, W.3    Stülke, J.4
  • 28
    • 0031443659 scopus 로고    scopus 로고
    • Loss of HMW1 and HMW3 in noncytadhering mutants of Mycoplasma pneumoniae occurs post-translationally
    • Popham, P. L., T. W. Hahn, K. A. Krebes, and D. C. Krause. 1997. Loss of HMW1 and HMW3 in noncytadhering mutants of Mycoplasma pneumoniae occurs post-translationally. Proc. Natl. Acad. Sci. U. S. A. 94:13979-13984.
    • (1997) Proc. Natl. Acad. Sci. U. S. A , vol.94 , pp. 13979-13984
    • Popham, P.L.1    Hahn, T.W.2    Krebes, K.A.3    Krause, D.C.4
  • 30
    • 54549099189 scopus 로고    scopus 로고
    • A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments
    • Shah, I. M., M. H. Laaberki, D. L. Popham, and J. Dworkin. 2008. A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments. Cell 135:486-496.
    • (2008) Cell , vol.135 , pp. 486-496
    • Shah, I.M.1    Laaberki, M.H.2    Popham, D.L.3    Dworkin, J.4
  • 31
    • 0036773364 scopus 로고    scopus 로고
    • A novel mode of control of Mycoplasma pneumoniae HPr kinase/phosphatase activity reflects its parasitic lifestyle
    • Steinhauer, K., T. Jepp, W. Hillen, and J. Stülke. 2002. A novel mode of control of Mycoplasma pneumoniae HPr kinase/phosphatase activity reflects its parasitic lifestyle. Microbiology 148:3277-3284.
    • (2002) Microbiology , vol.148 , pp. 3277-3284
    • Steinhauer, K.1    Jepp, T.2    Hillen, W.3    Stülke, J.4
  • 32
    • 73449131754 scopus 로고    scopus 로고
    • Mycoplasma and Spiroplasma
    • M. Schaechter ed, Elsevier, Oxford, United Kingdom
    • Stülke, J., H. Eilers, and S. R. Schmidl. 2009. Mycoplasma and Spiroplasma, p. 208-219. In M. Schaechter (ed.), Encyclopedia of microbiology. Elsevier, Oxford, United Kingdom.
    • (2009) Encyclopedia of microbiology , pp. 208-219
    • Stülke, J.1    Eilers, H.2    Schmidl, S.R.3
  • 33
    • 34547912457 scopus 로고    scopus 로고
    • Mapping phospho-proteins in Mycoplasma genitalium and Mycoplasma pneumoniae
    • Su, H. C., C. A. Hutchison, and M. C. Giddings. 2007. Mapping phospho-proteins in Mycoplasma genitalium and Mycoplasma pneumoniae. BMC Microbiol. 7:63.
    • (2007) BMC Microbiol , vol.7 , pp. 63
    • Su, H.C.1    Hutchison, C.A.2    Giddings, M.C.3
  • 34
    • 5644300391 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae and its role as a human pathogen
    • Waites, K. B., and D. F. Talkington. 2004. Mycoplasma pneumoniae and its role as a human pathogen. Clin. Microbiol. Rev. 17:697-728.
    • (2004) Clin. Microbiol. Rev , vol.17 , pp. 697-728
    • Waites, K.B.1    Talkington, D.F.2
  • 35
    • 10044248456 scopus 로고    scopus 로고
    • HMW1 is required for stability and localization of HMW2 to the attachment organelle of Mycoplasma pneumoniae
    • Willby, M. J., M. F. Balish, S. M. Ross, K. K. Lee, J. L. Jordan, and D. C. Krause. 2004. HMW1 is required for stability and localization of HMW2 to the attachment organelle of Mycoplasma pneumoniae. J. Bacteriol. 186:8221-8228.
    • (2004) J. Bacteriol , vol.186 , pp. 8221-8228
    • Willby, M.J.1    Balish, M.F.2    Ross, S.M.3    Lee, K.K.4    Jordan, J.L.5    Krause, D.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.