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Volumn 105, Issue 15, 2008, Pages 5891-5896

An essential sensor histidine kinase controlled by transmembrane helix interactions with its auxiliary proteins

Author keywords

Replica exchange molecular dynamics simulation; Signal transduction; YycG; YycH; YycI

Indexed keywords

PROTEIN HISTIDINE KINASE; PROTEIN HISTIDINE KINASE YYCH; PROTEIN HISTIDINE KINASE YYCL;

EID: 44449149782     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0800247105     Document Type: Article
Times cited : (78)

References (26)
  • 1
    • 33845640610 scopus 로고    scopus 로고
    • Stimulus perception in bacterial signal-transducing histidine kinases
    • Mascher T, Helmann JD, Unden G (2006) Stimulus perception in bacterial signal-transducing histidine kinases. Microbiol Mol Biol Rev 70:910-938.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 910-938
    • Mascher, T.1    Helmann, J.D.2    Unden, G.3
  • 2
    • 36549003158 scopus 로고    scopus 로고
    • Sensor complexes regulating two-component signal transduction
    • Szurmant H., White RA, Hoch JA (2007) Sensor complexes regulating two-component signal transduction. Curr Opin Struct Biol 17:706-715.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 706-715
    • Szurmant, H.1    White, R.A.2    Hoch, J.A.3
  • 3
    • 0031757758 scopus 로고    scopus 로고
    • A two-component signal transduction system essential for growth of Bacillus subtilis: Implications for anti-infective therapy
    • Fabret C, Hoch JA (1998) A two-component signal transduction system essential for growth of Bacillus subtilis: Implications for anti-infective therapy. J Bacteriol 180:6375-6383.
    • (1998) J Bacteriol , vol.180 , pp. 6375-6383
    • Fabret, C.1    Hoch, J.A.2
  • 4
    • 33748520597 scopus 로고    scopus 로고
    • MtrAB-LpqB: A conserved three-component system in actinobacteria?
    • Hoskisson PA, Hutchings MI (2006) MtrAB-LpqB: A conserved three-component system in actinobacteria? Trends Microbiol 14:444-449.
    • (2006) Trends Microbiol , vol.14 , pp. 444-449
    • Hoskisson, P.A.1    Hutchings, M.I.2
  • 5
    • 27144455733 scopus 로고    scopus 로고
    • Regulation of the pspA virulence factor and essential pcsB murein biosynthetic genes by the phosphorylated VicR (YycF) response regulator in Streptococcus pneumoniae
    • Ng WL, Tsui HC, Winkler ME (2005) Regulation of the pspA virulence factor and essential pcsB murein biosynthetic genes by the phosphorylated VicR (YycF) response regulator in Streptococcus pneumoniae. J Bacteriol 187:7444-7459.
    • (2005) J Bacteriol , vol.187 , pp. 7444-7459
    • Ng, W.L.1    Tsui, H.C.2    Winkler, M.E.3
  • 6
    • 34250632446 scopus 로고    scopus 로고
    • The essential YycFG two-component system controls cell wall metabolism in Bacillus subtilis
    • Bisicchia P, et al. (2007) The essential YycFG two-component system controls cell wall metabolism in Bacillus subtilis. Mol Microbiol 65:180-200.
    • (2007) Mol Microbiol , vol.65 , pp. 180-200
    • Bisicchia, P.1
  • 7
    • 36549008206 scopus 로고    scopus 로고
    • New insights into the WalK/WalR (YycG/YycF) essential signal transduction pathway reveal a major role in controlling cell wall metabolism and biofilm formation in Staphylococcus aureus
    • Dubrac S, Boneca IG, Poupel O, Msadek T (2007) New insights into the WalK/WalR (YycG/YycF) essential signal transduction pathway reveal a major role in controlling cell wall metabolism and biofilm formation in Staphylococcus aureus. J Bacteriol 189:8257-8269.
    • (2007) J Bacteriol , vol.189 , pp. 8257-8269
    • Dubrac, S.1    Boneca, I.G.2    Poupel, O.3    Msadek, T.4
  • 8
    • 0033940185 scopus 로고    scopus 로고
    • The essential two-component regulatory system encoded by yycF and yycG modulates expression of the ftsAZ operon in Bacillus subtilis
    • Fukuchi K, et al. (2000) The essential two-component regulatory system encoded by yycF and yycG modulates expression of the ftsAZ operon in Bacillus subtilis. Microbiology 146 (Pt 7):1573-1583.
    • (2000) Microbiology , vol.146 , Issue.PART 7 , pp. 1573-1583
    • Fukuchi, K.1
  • 9
    • 34247849321 scopus 로고    scopus 로고
    • YycH and YycI interact to regulate the essential YycFG two-component system in Bacillus subtilis
    • Szurmant H, Mohan MA, Imus PM, Hoch JA (2007) YycH and YycI interact to regulate the essential YycFG two-component system in Bacillus subtilis. J Bacteriol 189:3280-3289.
    • (2007) J Bacteriol , vol.189 , pp. 3280-3289
    • Szurmant, H.1    Mohan, M.A.2    Imus, P.M.3    Hoch, J.A.4
  • 10
    • 22544460491 scopus 로고    scopus 로고
    • YycH regulates the activity of the essential YycFG two-component system in Bacillus subtilis
    • Szurmant H, Nelson K, Kim EJ, Perego M, Hoch JA (2005) YycH regulates the activity of the essential YycFG two-component system in Bacillus subtilis. J Bacteriol 187:5419-5426.
    • (2005) J Bacteriol , vol.187 , pp. 5419-5426
    • Szurmant, H.1    Nelson, K.2    Kim, E.J.3    Perego, M.4    Hoch, J.A.5
  • 11
    • 34247892343 scopus 로고    scopus 로고
    • The crystal structure of Bacillus subtilis YycI reveals a common fold for two members of an unusual class of sensor histidine kinase regulatory proteins
    • Santelli E, Liddington RC, Mohan MA, Hoch JA, Szurmant H (2007) The crystal structure of Bacillus subtilis YycI reveals a common fold for two members of an unusual class of sensor histidine kinase regulatory proteins. J Bacteriol 189:3290-3295.
    • (2007) J Bacteriol , vol.189 , pp. 3290-3295
    • Santelli, E.1    Liddington, R.C.2    Mohan, M.A.3    Hoch, J.A.4    Szurmant, H.5
  • 12
    • 33645533419 scopus 로고    scopus 로고
    • The crystal structure of YycH involved in the regulation of the essential YycFG two-component system in Bacillus subtilis reveals a novel tertiary structure
    • Szurmant H, Zhao H, Mohan MA, Hoch JA, Varughese KI (2006) The crystal structure of YycH involved in the regulation of the essential YycFG two-component system in Bacillus subtilis reveals a novel tertiary structure. Protein Sci 15:929-934.
    • (2006) Protein Sci , vol.15 , pp. 929-934
    • Szurmant, H.1    Zhao, H.2    Mohan, M.A.3    Hoch, J.A.4    Varughese, K.I.5
  • 13
    • 33846804141 scopus 로고    scopus 로고
    • Membrane assembly of simple helix homo-oligomers studied via molecular dynamics simulations
    • Bu L, Im W, Brooks CL, II (2007) Membrane assembly of simple helix homo-oligomers studied via molecular dynamics simulations. Biophys J 92:854-863.
    • (2007) Biophys J , vol.92 , pp. 854-863
    • Bu, L.1    Im, W.2    Brooks II, C.L.3
  • 14
    • 6444243998 scopus 로고    scopus 로고
    • Singular structures and operon organizations of essential two-component systems in species of Streptococcus
    • Ng WL, Winkler ME (2004) Singular structures and operon organizations of essential two-component systems in species of Streptococcus. Microbiology 150:3096-3098.
    • (2004) Microbiology , vol.150 , pp. 3096-3098
    • Ng, W.L.1    Winkler, M.E.2
  • 15
    • 33748183257 scopus 로고    scopus 로고
    • The HAMP domain structure implies helix rotation in transmembrane signaling
    • Hulko M, et al. (2006) The HAMP domain structure implies helix rotation in transmembrane signaling. Cell 126:929-940.
    • (2006) Cell , vol.126 , pp. 929-940
    • Hulko, M.1
  • 16
    • 36848998769 scopus 로고    scopus 로고
    • Structure of the conserved HAMP domain in an intact, membrane-bound chemoreceptor: A disulfide mapping study
    • Swain KE, Falke JJ (2007) Structure of the conserved HAMP domain in an intact, membrane-bound chemoreceptor: A disulfide mapping study. Biochemistry 46:13684-13695.
    • (2007) Biochemistry , vol.46 , pp. 13684-13695
    • Swain, K.E.1    Falke, J.J.2
  • 17
    • 0042931286 scopus 로고    scopus 로고
    • Sequence motifs, polar interactions and conformational changes in helical membrane proteins
    • Curran AR, Engelman DM (2003) Sequence motifs, polar interactions and conformational changes in helical membrane proteins. Curr Opin Struct Biol 13:412-417.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 412-417
    • Curran, A.R.1    Engelman, D.M.2
  • 18
    • 2942748593 scopus 로고    scopus 로고
    • Bacterial chemosensing: Cooperative molecular logic
    • Wolanin PM, Stock JB (2004) Bacterial chemosensing: cooperative molecular logic. Curr Biol 14:R486-R487.
    • (2004) Curr Biol , vol.14
    • Wolanin, P.M.1    Stock, J.B.2
  • 19
    • 0023849547 scopus 로고
    • Transcription of Bacillus subtilis subtilisin and expression of subtilisin in sporulation mutants
    • Ferrari E, Henner DJ, Perego M, Hoch JA (1988) Transcription of Bacillus subtilis subtilisin and expression of subtilisin in sporulation mutants. J Bacteriol 170:289-295.
    • (1988) J Bacteriol , vol.170 , pp. 289-295
    • Ferrari, E.1    Henner, D.J.2    Perego, M.3    Hoch, J.A.4
  • 22
    • 0031578972 scopus 로고    scopus 로고
    • Parallel tempering algorithm for conformational studies of biological molecules
    • Hansmann UHE (1997) Parallel tempering algorithm for conformational studies of biological molecules. Chem Phys Lett 281:140-150.
    • (1997) Chem Phys Lett , vol.281 , pp. 140-150
    • Hansmann, U.H.E.1
  • 23
    • 1942423619 scopus 로고    scopus 로고
    • MMTSB Tool Set: Enhanced sampling and multiscale modeling methods for applications in structural biology
    • Feig M, Karanicolas J, Brooks CL, III (2004) MMTSB Tool Set: Enhanced sampling and multiscale modeling methods for applications in structural biology. J Mol Graphics Model 22:377-395.
    • (2004) J Mol Graphics Model , vol.22 , pp. 377-395
    • Feig, M.1    Karanicolas, J.2    Brooks III, C.L.3
  • 24
    • 0242322528 scopus 로고    scopus 로고
    • An implicit membrane generalized born theory for the study of structure, stability, and interactions of membrane proteins
    • Im W, Feig M, Brooks CL, III (2003) An implicit membrane generalized born theory for the study of structure, stability, and interactions of membrane proteins. Biophys J 85:2900-2918.
    • (2003) Biophys J , vol.85 , pp. 2900-2918
    • Im, W.1    Feig, M.2    Brooks III, C.L.3
  • 25
    • 84986512474 scopus 로고
    • CHARMM: A program for macromolecular energy, minimization, and dynamics calculations
    • Brooks BR, et al. (1983) CHARMM: A program for macromolecular energy, minimization, and dynamics calculations. J Compu Chem 4:187-217.
    • (1983) J Compu Chem , vol.4 , pp. 187-217
    • Brooks, B.R.1
  • 26
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • MacKerell AD, et al. (1998) All-atom empirical potential for molecular modeling and dynamics studies of proteins. J Phys Chem B 102:3586-3616.
    • (1998) J Phys Chem B , vol.102 , pp. 3586-3616
    • MacKerell, A.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.