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Volumn 447, Issue 1, 2014, Pages 165-171

A novel mode of regulation of the Staphylococcus aureus Vancomycin-resistance-associated response regulator VraR mediated by Stk1 protein phosphorylation

Author keywords

Antibiotic resistance; Phosphorylation; Ser Thr protein kinase; Staphylococcus aureus; VraR

Indexed keywords

PROTEIN SERINE THREONINE KINASE; REGULATOR PROTEIN; STK1 PROTEIN; UNCLASSIFIED DRUG; VANCOMYCIN RESISTANCE ASSOCIATED RESPONSE REGULATOR;

EID: 84899483277     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2014.03.128     Document Type: Article
Times cited : (39)

References (26)
  • 1
    • 73649088602 scopus 로고    scopus 로고
    • The impact of serine/threonine phosphorylation in Staphylococcus aureus
    • K. Ohlsen, and S. Donat The impact of serine/threonine phosphorylation in Staphylococcus aureus Int. J. Med. Microbiol. 300 2010 137 141
    • (2010) Int. J. Med. Microbiol. , vol.300 , pp. 137-141
    • Ohlsen, K.1    Donat, S.2
  • 2
    • 67649401960 scopus 로고    scopus 로고
    • Transcriptome and functional analysis of the eukaryotic-type serine/threonine kinase PknB in Staphylococcus aureus
    • S. Donat, K. Streker, T. Schirmeister, S. Rakette, T. Stehle, M. Liebeke, M. Lalk, and K. Ohlsen Transcriptome and functional analysis of the eukaryotic-type serine/threonine kinase PknB in Staphylococcus aureus J. Bacteriol. 191 2009 4056 4069
    • (2009) J. Bacteriol. , vol.191 , pp. 4056-4069
    • Donat, S.1    Streker, K.2    Schirmeister, T.3    Rakette, S.4    Stehle, T.5    Liebeke, M.6    Lalk, M.7    Ohlsen, K.8
  • 3
    • 77950489158 scopus 로고    scopus 로고
    • Phosphorylation of the virulence regulator SarA modulates its ability to bind DNA in Staphylococcus aureus
    • J.P. Didier, A.J. Cozzone, and B. Duclos Phosphorylation of the virulence regulator SarA modulates its ability to bind DNA in Staphylococcus aureus FEMS Microbiol. Lett. 306 2010 30 36
    • (2010) FEMS Microbiol. Lett. , vol.306 , pp. 30-36
    • Didier, J.P.1    Cozzone, A.J.2    Duclos, B.3
  • 5
    • 78649361924 scopus 로고    scopus 로고
    • The Staphylococcus aureus autoinducer-2 synthase LuxS is regulated by Ser/Thr phosphorylation
    • M.E. Cluzel, I. Zanella-Cleon, A.J. Cozzone, K. Futterer, B. Duclos, and V. Molle The Staphylococcus aureus autoinducer-2 synthase LuxS is regulated by Ser/Thr phosphorylation J. Bacteriol. 192 2010 6295 6301
    • (2010) J. Bacteriol. , vol.192 , pp. 6295-6301
    • Cluzel, M.E.1    Zanella-Cleon, I.2    Cozzone, A.J.3    Futterer, K.4    Duclos, B.5    Molle, V.6
  • 6
    • 84871547788 scopus 로고    scopus 로고
    • A novel mode of regulation of the Staphylococcus aureus catabolite control protein A (CcpA) mediated by Stk1 protein phosphorylation
    • J. Leiba, T. Hartmann, M.E. Cluzel, M. Cohen-Gonsaud, F. Delolme, M. Bischoff, and V. Molle A novel mode of regulation of the Staphylococcus aureus catabolite control protein A (CcpA) mediated by Stk1 protein phosphorylation J. Biol. Chem. 287 2012 43607 43619
    • (2012) J. Biol. Chem. , vol.287 , pp. 43607-43619
    • Leiba, J.1    Hartmann, T.2    Cluzel, M.E.3    Cohen-Gonsaud, M.4    Delolme, F.5    Bischoff, M.6    Molle, V.7
  • 7
    • 78651543474 scopus 로고    scopus 로고
    • Induction kinetics of the Staphylococcus aureus cell wall stress stimulon in response to different cell wall active antibiotics
    • V. Dengler, P.S. Meier, R. Heusser, B. Berger-Bachi, and N. McCallum Induction kinetics of the Staphylococcus aureus cell wall stress stimulon in response to different cell wall active antibiotics BMC Microbiol. 11 2011 16
    • (2011) BMC Microbiol. , vol.11 , pp. 16
    • Dengler, V.1    Meier, P.S.2    Heusser, R.3    Berger-Bachi, B.4    McCallum, N.5
  • 8
    • 84860894256 scopus 로고    scopus 로고
    • Genetic pathway in acquisition and loss of vancomycin resistance in a methicillin resistant Staphylococcus aureus (MRSA) strain of clonal type USA300
    • S. Gardete, C. Kim, B.M. Hartmann, M. Mwangi, C.M. Roux, P.M. Dunman, H.F. Chambers, and A. Tomasz Genetic pathway in acquisition and loss of vancomycin resistance in a methicillin resistant Staphylococcus aureus (MRSA) strain of clonal type USA300 PLoS Pathog. 8 2012 e1002505
    • (2012) PLoS Pathog. , vol.8 , pp. 1002505
    • Gardete, S.1    Kim, C.2    Hartmann, B.M.3    Mwangi, M.4    Roux, C.M.5    Dunman, P.M.6    Chambers, H.F.7    Tomasz, A.8
  • 9
    • 84872022846 scopus 로고    scopus 로고
    • VraT/YvqF is required for methicillin resistance and activation of the VraSR regulon in Staphylococcus aureus
    • S. Boyle-Vavra, S. Yin, D.S. Jo, C.P. Montgomery, and R.S. Daum VraT/YvqF is required for methicillin resistance and activation of the VraSR regulon in Staphylococcus aureus Antimicrob. Agents Chemother. 57 2013 83 95
    • (2013) Antimicrob. Agents Chemother. , vol.57 , pp. 83-95
    • Boyle-Vavra, S.1    Yin, S.2    Jo, D.S.3    Montgomery, C.P.4    Daum, R.S.5
  • 10
    • 79651470151 scopus 로고    scopus 로고
    • Mutational analyses of open reading frames within the vraSR operon and their roles in the cell wall stress response of Staphylococcus aureus
    • N. McCallum, P.S. Meier, R. Heusser, and B. Berger-Bachi Mutational analyses of open reading frames within the vraSR operon and their roles in the cell wall stress response of Staphylococcus aureus Antimicrob. Agents Chemother. 55 2011 1391 1402
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 1391-1402
    • McCallum, N.1    Meier, P.S.2    Heusser, R.3    Berger-Bachi, B.4
  • 11
    • 79952357437 scopus 로고    scopus 로고
    • Site-specific mutation of Staphylococcus aureus VraS reveals a crucial role for the VraR-VraS sensor in the emergence of glycopeptide resistance
    • E. Galbusera, A. Renzoni, D.O. Andrey, A. Monod, C. Barras, P. Tortora, A. Polissi, and W.L. Kelley Site-specific mutation of Staphylococcus aureus VraS reveals a crucial role for the VraR-VraS sensor in the emergence of glycopeptide resistance Antimicrob. Agents Chemother. 55 2011 1008 1020
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 1008-1020
    • Galbusera, E.1    Renzoni, A.2    Andrey, D.O.3    Monod, A.4    Barras, C.5    Tortora, P.6    Polissi, A.7    Kelley, W.L.8
  • 12
    • 49949091451 scopus 로고    scopus 로고
    • PETPhos: A customized expression vector designed for further characterization of Ser/Thr/Tyr protein kinases and their substrates
    • M.J. Canova, L. Kremer, and V. Molle pETPhos: a customized expression vector designed for further characterization of Ser/Thr/Tyr protein kinases and their substrates Plasmid 60 2008 149 153
    • (2008) Plasmid , vol.60 , pp. 149-153
    • Canova, M.J.1    Kremer, L.2    Molle, V.3
  • 13
    • 78049378075 scopus 로고    scopus 로고
    • An improved method to unravel phosphoacceptors in Ser/Thr protein kinase-phosphorylated substrates
    • V. Molle, J. Leiba, I. Zanella-Cleon, M. Becchi, and L. Kremer An improved method to unravel phosphoacceptors in Ser/Thr protein kinase-phosphorylated substrates Proteomics 10 2010 3910 3915
    • (2010) Proteomics , vol.10 , pp. 3910-3915
    • Molle, V.1    Leiba, J.2    Zanella-Cleon, I.3    Becchi, M.4    Kremer, L.5
  • 15
    • 45549091606 scopus 로고    scopus 로고
    • A close-up view of the VraSR two-component system. A mediator of Staphylococcus aureus response to cell wall damage
    • A. Belcheva, and D. Golemi-Kotra A close-up view of the VraSR two-component system. A mediator of Staphylococcus aureus response to cell wall damage J. Biol. Chem. 283 2008 12354 12364
    • (2008) J. Biol. Chem. , vol.283 , pp. 12354-12364
    • Belcheva, A.1    Golemi-Kotra, D.2
  • 16
    • 80052270882 scopus 로고    scopus 로고
    • Negative regulation by Ser/Thr phosphorylation of HadAB and HadBC dehydratases from Mycobacterium tuberculosis type II fatty acid synthase system
    • N. Slama, J. Leiba, N. Eynard, M. Daffe, L. Kremer, A. Quemard, and V. Molle Negative regulation by Ser/Thr phosphorylation of HadAB and HadBC dehydratases from Mycobacterium tuberculosis type II fatty acid synthase system Biochem. Biophys. Res. Commun. 412 2011 401 406
    • (2011) Biochem. Biophys. Res. Commun. , vol.412 , pp. 401-406
    • Slama, N.1    Leiba, J.2    Eynard, N.3    Daffe, M.4    Kremer, L.5    Quemard, A.6    Molle, V.7
  • 17
    • 80052540898 scopus 로고    scopus 로고
    • The sigmaB-dependent yabJ-spoVG operon is involved in the regulation of extracellular nuclease, lipase, and protease expression in Staphylococcus aureus
    • B. Schulthess, D.A. Bloes, P. Francois, M. Girard, J. Schrenzel, M. Bischoff, and B. Berger-Bachi The sigmaB-dependent yabJ-spoVG operon is involved in the regulation of extracellular nuclease, lipase, and protease expression in Staphylococcus aureus J. Bacteriol. 193 2011 4954 4962
    • (2011) J. Bacteriol. , vol.193 , pp. 4954-4962
    • Schulthess, B.1    Bloes, D.A.2    Francois, P.3    Girard, M.4    Schrenzel, J.5    Bischoff, M.6    Berger-Bachi, B.7
  • 18
    • 77955293898 scopus 로고    scopus 로고
    • The role of PknB kinase in antibiotic resistance and virulence in community acquired methicillin resistant Staphylococcus aureus strain USA300
    • S. Tamber, J. Schwartzman, and A.L. Cheung The role of PknB kinase in antibiotic resistance and virulence in community acquired methicillin resistant Staphylococcus aureus strain USA300 Infect. Immun. 78 2010 3637 3646
    • (2010) Infect. Immun. , vol.78 , pp. 3637-3646
    • Tamber, S.1    Schwartzman, J.2    Cheung, A.L.3
  • 20
    • 77952057697 scopus 로고    scopus 로고
    • Phosphorylation of MgrA and its effect on expression of the NorA and NorB efflux pumps of Staphylococcus aureus
    • Q.C. Truong-Bolduc, and D.C. Hooper Phosphorylation of MgrA and its effect on expression of the NorA and NorB efflux pumps of Staphylococcus aureus J. Bacteriol. 192 2010 2525 2534
    • (2010) J. Bacteriol. , vol.192 , pp. 2525-2534
    • Truong-Bolduc, Q.C.1    Hooper, D.C.2
  • 22
    • 73349138284 scopus 로고    scopus 로고
    • Separation and detection of large phosphoproteins using Phos-tag SDS-PAGE
    • E. Kinoshita, E. Kinoshita-Kikuta, and T. Koike Separation and detection of large phosphoproteins using Phos-tag SDS-PAGE Nat. Protoc. 4 2009 1513 1521
    • (2009) Nat. Protoc. , vol.4 , pp. 1513-1521
    • Kinoshita, E.1    Kinoshita-Kikuta, E.2    Koike, T.3
  • 23
    • 84877840614 scopus 로고    scopus 로고
    • Phosphorylation-dependent localization of the response regulator FrzZ signals cell reversals in Myxococcus xanthus
    • C. Kaimer, and D.R. Zusman Phosphorylation-dependent localization of the response regulator FrzZ signals cell reversals in Myxococcus xanthus Mol. Microbiol. 88 2013 740 753
    • (2013) Mol. Microbiol. , vol.88 , pp. 740-753
    • Kaimer, C.1    Zusman, D.R.2
  • 24
    • 84878143682 scopus 로고    scopus 로고
    • Phosphorylation-dependent conformational changes and domain rearrangements in Staphylococcus aureus VraR activation
    • P.G. Leonard, D. Golemi-Kotra, and A.M. Stock Phosphorylation-dependent conformational changes and domain rearrangements in Staphylococcus aureus VraR activation Proc. Natl. Acad. Sci. U.S.A. 110 2013 8525 8530
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 8525-8530
    • Leonard, P.G.1    Golemi-Kotra, D.2    Stock, A.M.3
  • 25
    • 40849134012 scopus 로고    scopus 로고
    • The NMR structure of the Staphylococcus aureus response regulator VraR DNA binding domain reveals a dynamic relationship between it and its associated receiver domain
    • L.W. Donaldson The NMR structure of the Staphylococcus aureus response regulator VraR DNA binding domain reveals a dynamic relationship between it and its associated receiver domain Biochemistry 47 2008 3379 3388
    • (2008) Biochemistry , vol.47 , pp. 3379-3388
    • Donaldson, L.W.1
  • 26
    • 84872325218 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis S-adenosyl-l-homocysteine hydrolase is negatively regulated by Ser/Thr phosphorylation
    • R.M. Corrales, J. Leiba, M. Cohen-Gonsaud, V. Molle, and L. Kremer Mycobacterium tuberculosis S-adenosyl-l-homocysteine hydrolase is negatively regulated by Ser/Thr phosphorylation Biochem. Biophys. Res. Commun. 430 2012 858 864
    • (2012) Biochem. Biophys. Res. Commun. , vol.430 , pp. 858-864
    • Corrales, R.M.1    Leiba, J.2    Cohen-Gonsaud, M.3    Molle, V.4    Kremer, L.5


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