메뉴 건너뛰기




Volumn 188, Issue 21, 2006, Pages 7328-7330

A new perspective on response regulator activation

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PROTEIN CHEY; PROTEIN CHEZ; PROTEIN FLIM; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 33750478377     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01268-06     Document Type: Note
Times cited : (57)

References (25)
  • 2
    • 0032739281 scopus 로고    scopus 로고
    • C-terminal DNA binding stimulates N-terminal phosphorylation of the outer membrane protein regulator OmpR from Escherichia coli
    • Ames, S. K., N. Frankema, and L. J. Kenney. 1999. C-terminal DNA binding stimulates N-terminal phosphorylation of the outer membrane protein regulator OmpR from Escherichia coli. Proc. Natl. Acad. Sci. USA 96:11792-11797.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11792-11797
    • Ames, S.K.1    Frankema, N.2    Kenney, L.J.3
  • 3
    • 0026572085 scopus 로고
    • Correlation between phosphorylation of the chemotaxis protein CheY and its activity at the flagellar motor
    • Barak, R., and M. Eisenbach. 1992. Correlation between phosphorylation of the chemotaxis protein CheY and its activity at the flagellar motor. Biochemistry 31:1821-1826.
    • (1992) Biochemistry , vol.31 , pp. 1821-1826
    • Barak, R.1    Eisenbach, M.2
  • 7
    • 0036838267 scopus 로고    scopus 로고
    • Genetic analysis of response regulator activation in bacterial chemotaxis suggests an intermolecular mechanism
    • Da Re, S., T. Tolstykh, P. M. Wolanin, and J. B. Stock. 2002. Genetic analysis of response regulator activation in bacterial chemotaxis suggests an intermolecular mechanism. Protein Sci. 11:2644-2654.
    • (2002) Protein Sci. , vol.11 , pp. 2644-2654
    • Da Re, S.1    Tolstykh, T.2    Wolanin, P.M.3    Stock, J.B.4
  • 8
    • 33750435591 scopus 로고    scopus 로고
    • Switched or not? The structure of unphosphorylated CheY bound to the N terminus of FliM
    • Dyer, C. M., and F. W. Dahlquist. 2006. Switched or not? The structure of unphosphorylated CheY bound to the N terminus of FliM. J. Bacteriol. 188:7354-7363.
    • (2006) J. Bacteriol. , vol.188 , pp. 7354-7363
    • Dyer, C.M.1    Dahlquist, F.W.2
  • 9
    • 33646776723 scopus 로고    scopus 로고
    • Reconciling the "old" and "new" views of protein allostery: A molecular simulation study of chemotaxis Y protein (CheY)
    • Formaneck, M. S., L. Ma, and Q. Cui. 2006. Reconciling the "old" and "new" views of protein allostery: a molecular simulation study of chemotaxis Y protein (CheY). Proteins 63:846-867.
    • (2006) Proteins , vol.63 , pp. 846-867
    • Formaneck, M.S.1    Ma, L.2    Cui, Q.3
  • 10
    • 23944523895 scopus 로고    scopus 로고
    • A census of membrane-bound and intracellular signal transduction proteins in bacteria: Bacterial IQ, extroverts and introverts
    • Galperin, M. Y. 2005. A census of membrane-bound and intracellular signal transduction proteins in bacteria: bacterial IQ, extroverts and introverts. BMC Microbiol. 5:35.
    • (2005) BMC Microbiol. , vol.5 , pp. 35
    • Galperin, M.Y.1
  • 11
    • 33646767505 scopus 로고    scopus 로고
    • Crystal structures of beryllium fluoride-free and beryllium fluoride-bound CheY in complex with the conserved C-terminal peptide of CheZ reveal dual binding modes specific to CheY conformation
    • Guhaniyogi, J., V. L. Robinson, and A. M. Stock. 2006. Crystal structures of beryllium fluoride-free and beryllium fluoride-bound CheY in complex with the conserved C-terminal peptide of CheZ reveal dual binding modes specific to CheY conformation. J. Mol. Biol. 359:624-645.
    • (2006) J. Mol. Biol. , vol.359 , pp. 624-645
    • Guhaniyogi, J.1    Robinson, V.L.2    Stock, A.M.3
  • 12
    • 0033599026 scopus 로고    scopus 로고
    • Structure of a transiently phosphorylated switch in bacterial signal transduction
    • Kern, D., B. F. Volkman, P. Luginbuhl, M. J. Nohaile, S. Kustu, and D. E. Wemmer. 1999. Structure of a transiently phosphorylated switch in bacterial signal transduction. Nature 40:894-898.
    • (1999) Nature , vol.40 , pp. 894-898
    • Kern, D.1    Volkman, B.F.2    Luginbuhl, P.3    Nohaile, M.J.4    Kustu, S.5    Wemmer, D.E.6
  • 16
    • 0027207516 scopus 로고
    • Is acetyl phosphate a global signal in Escherichia coli?
    • McCleary, W. R., J. B. Stock, and A. J. Ninfa. 1993. Is acetyl phosphate a global signal in Escherichia coli? J. Bacteriol. 175:2793-2798.
    • (1993) J. Bacteriol. , vol.175 , pp. 2793-2798
    • McCleary, W.R.1    Stock, J.B.2    Ninfa, A.J.3
  • 17
    • 0033603635 scopus 로고    scopus 로고
    • Identification of the binding interfaces on CheY for two of its targets, the phosphatase CheZ and the flagellar switch protein FliM
    • McEvoy, M. M., A. Bren, M. Eisenbach, and F. W. Dahlquist. 1999. Identification of the binding interfaces on CheY for two of its targets, the phosphatase CheZ and the flagellar switch protein FliM. J. Mol. Biol. 289:1423-1433.
    • (1999) J. Mol. Biol. , vol.289 , pp. 1423-1433
    • McEvoy, M.M.1    Bren, A.2    Eisenbach, M.3    Dahlquist, F.W.4
  • 18
    • 0033887436 scopus 로고    scopus 로고
    • A tale of two components: A novel kinase and a regulatory switch
    • Robinson, V. L., D. R. Buckler, and A. M. Stock. 2000. A tale of two components: a novel kinase and a regulatory switch. Nat. Struct. Biol. 7:628-633.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 628-633
    • Robinson, V.L.1    Buckler, D.R.2    Stock, A.M.3
  • 19
    • 0035933040 scopus 로고    scopus 로고
    • Conformational coupling in the chemotaxis response regulator CheY
    • Schuster, M., R. E. Silversmith, and R. B. Bourret. 2001. Conformational coupling in the chemotaxis response regulator CheY. Proc. Natl. Acad. Sci. USA 98:6003-6008.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6003-6008
    • Schuster, M.1    Silversmith, R.E.2    Bourret, R.B.3
  • 20
    • 0035800848 scopus 로고    scopus 로고
    • A distinct meta-active conformation in the 1.1-Å resolution structure of wild-type apoCheY
    • Simonovic, M., and K. Volz. 2001. A distinct meta-active conformation in the 1.1-Å resolution structure of wild-type apoCheY. J. Biol. Chem. 276:28637-28640.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28637-28640
    • Simonovic, M.1    Volz, K.2
  • 21
    • 28844432653 scopus 로고    scopus 로고
    • A common dimerization interface in bacterial response regulators KdpE and TorR
    • Toro-Roman, A., T. Wu, and A. M. Stock. 2005. A common dimerization interface in bacterial response regulators KdpE and TorR. Protein Sci. 14:3077-3088.
    • (2005) Protein Sci. , vol.14 , pp. 3077-3088
    • Toro-Roman, A.1    Wu, T.2    Stock, A.M.3
  • 22
    • 0035937443 scopus 로고    scopus 로고
    • Two-state allosteric behavior in a single domain signaling protein
    • Volkman, B. F., D. Lipson, D. E. Wemmer, and D. Kern. 2001. Two-state allosteric behavior in a single domain signaling protein. Science 291:2429-2433.
    • (2001) Science , vol.291 , pp. 2429-2433
    • Volkman, B.F.1    Lipson, D.2    Wemmer, D.E.3    Kern, D.4
  • 23
    • 0027517812 scopus 로고
    • Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria
    • Welch, M., K. Oosawa, S.-I. Aizawa, and M. Eisenbach. 1993. Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria. Proc. Natl. Acad. Sci. USA 90:8787-8791.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8787-8791
    • Welch, M.1    Oosawa, K.2    Aizawa, S.-I.3    Eisenbach, M.4
  • 24
    • 0035369115 scopus 로고    scopus 로고
    • Histidine kinases and response regulator proteins in two-component signaling systems
    • West, A. H., and A. M. Stock. 2001. Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem. Sci. 26:369-376.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 369-376
    • West, A.H.1    Stock, A.M.2
  • 25
    • 0031058440 scopus 로고    scopus 로고
    • Crystal structures of CheY mutants Y106W and T871/Y106W: CheY activation correlates with movement of residue 106
    • Zhu, X., J. Rebello, P. Matsumura, and K. Volz. 1997. Crystal structures of CheY mutants Y106W and T871/Y106W: CheY activation correlates with movement of residue 106. J. Biol. Chem. 272:5000-5006.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5000-5006
    • Zhu, X.1    Rebello, J.2    Matsumura, P.3    Volz, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.