메뉴 건너뛰기




Volumn 40, Issue 21, 2012, Pages 11073-11085

Structural insight of a concentration-dependent mechanism by which YdiV inhibits Escherichia coli flagellum biogenesis and motility

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PROTEIN FLHD2; PROTEIN FLHD4C2; PROTEIN YDIV; PROTEIN YDIV2; PROTEIN YDIV3; PROTEIN YDIV4; UNCLASSIFIED DRUG;

EID: 84870597147     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gks869     Document Type: Article
Times cited : (31)

References (47)
  • 1
    • 0036221998 scopus 로고    scopus 로고
    • Regulation of flagellar assembly
    • DOI 10.1016/S1369-5274(02)00302-8
    • Aldridge, P. and Hughes, K.T. (2002) Regulation of flagellar assembly. Curr. Opin. Microbiol., 5, 160-165. (Pubitemid 34289923)
    • (2002) Current Opinion in Microbiology , vol.5 , Issue.2 , pp. 160-165
    • Aldridge, P.1    Hughes, K.T.2
  • 2
    • 43849098574 scopus 로고    scopus 로고
    • Coordinating assembly of a bacterial macromolecular machine
    • DOI 10.1038/nrmicro1887, PII NRMICRO1887
    • Chevance, F.F. and Hughes, K.T. (2008) Coordinating assembly of a bacterial macromolecular machine. Nat. Rev. Microbiol., 6, 455-465. (Pubitemid 351696439)
    • (2008) Nature Reviews Microbiology , vol.6 , Issue.6 , pp. 455-465
    • Chevance, F.F.V.1    Hughes, K.T.2
  • 3
    • 0028132187 scopus 로고
    • The FlhD/FlhC complex, a transcriptional activator of the Escherichia coli flagellar class II operons
    • Liu, X. and Matsumura, P. (1994) The FlhD/FlhC complex, a transcriptional activator of the Escherichia coli flagellar class II operons. J. Bacteriol., 176, 7345-7351. (Pubitemid 24364062)
    • (1994) Journal of Bacteriology , vol.176 , Issue.23 , pp. 7345-7351
    • Liu, X.1    Matsumura, P.2
  • 4
    • 0037226537 scopus 로고    scopus 로고
    • FlhD/FlhC is a regulator of anaerobic respiration and the Entner-Doudoroff pathway through induction of the methyl-accepting chemotaxis protein Aer
    • DOI 10.1128/JB.185.2.534-543.2003
    • Pruss, B.M., Campbell, J.W., Van Dyk, T.K., Zhu, C., Kogan, Y. and Matsumura, P. (2003) FlhD/FlhC is a regulator of anaerobic respiration and the Entner-Doudoroff pathway through induction of the methyl-accepting chemotaxis protein Aer. J. Bacteriol., 185, 534-543. (Pubitemid 36070480)
    • (2003) Journal of Bacteriology , vol.185 , Issue.2 , pp. 534-543
    • Pruss, B.M.1    Campbell, J.W.2    Van Dyk, T.K.3    Zhu, C.4    Kogan, Y.5    Matsumura, P.6
  • 5
    • 0034601918 scopus 로고    scopus 로고
    • Functions of the subunits in the FlhD(2)C(2) transcriptional master regulator of bacterial flagellum biogenesis and swarming
    • Claret, L. and Hughes, C. (2000) Functions of the subunits in the FlhD(2)C(2) transcriptional master regulator of bacterial flagellum biogenesis and swarming. J. Mol. Biol., 303, 467-478.
    • (2000) J. Mol. Biol. , vol.303 , pp. 467-478
    • Claret, L.1    Hughes, C.2
  • 6
    • 0036386339 scopus 로고    scopus 로고
    • Interaction of the atypical prokaryotic transcription activator FlhD2C2 with early promoters of the flagellar gene hierarchy
    • Claret, L. and Hughes, C. (2002) Interaction of the atypical prokaryotic transcription activator FlhD2C2 with early promoters of the flagellar gene hierarchy. J. Mol. Biol., 321, 185-199.
    • (2002) J. Mol. Biol. , vol.321 , pp. 185-199
    • Claret, L.1    Hughes, C.2
  • 7
    • 29144451307 scopus 로고    scopus 로고
    • Structure of the Escherichia coli FlhDC complex, a prokaryotic heteromeric regulator of transcription
    • DOI 10.1016/j.jmb.2005.11.020, PII S0022283605014063
    • Wang, S., Fleming, R.T., Westbrook, E.M., Matsumura, P. and McKay, D.B. (2006) Structure of the Escherichia coli FlhDC complex, a prokaryotic heteromeric regulator of transcription. J. Mol. Biol., 355, 798-808. (Pubitemid 41817637)
    • (2006) Journal of Molecular Biology , vol.355 , Issue.4 , pp. 798-808
    • Wang, S.1    Fleming, R.T.2    Westbrook, E.M.3    Matsumura, P.4    McKay, D.B.5
  • 8
    • 0032796421 scopus 로고    scopus 로고
    • Multiple control of flagellum biosynthesis in Escherichia coli: Role of H-NS protein and the cyclic AMP-catabolite activator protein complex in transcription of the flhDC master operon
    • Soutourina, O., Kolb, A., Krin, E., Laurent-Winter, C., Rimsky, S., Danchin, A. and Bertin, P. (1999) Multiple control of flagellum biosynthesis in Escherichia coli: role of H-NS protein and the cyclic AMP-catabolite activator protein complex in transcription of the flhDC master operon. J. Bacteriol., 181, 7500-7508.
    • (1999) J. Bacteriol. , vol.181 , pp. 7500-7508
    • Soutourina, O.1    Kolb, A.2    Krin, E.3    Laurent-Winter, C.4    Rimsky, S.5    Danchin, A.6    Bertin, P.7
  • 9
    • 0035048862 scopus 로고    scopus 로고
    • Positive regulation of motility and flhDC expression by the RNA-binding protein CsrA of Escherichia coli
    • DOI 10.1046/j.1365-2958.2001.02380.x
    • Wei, B.L., Brun-Zinkernagel, A.M., Simecka, J.W., Pruss, B.M., Babitzke, P. and Romeo, T. (2001) Positive regulation of motility and flhDC expression by the RNA-binding protein CsrA of Escherichia coli. Mol. Microbiol., 40, 245-256. (Pubitemid 32322877)
    • (2001) Molecular Microbiology , vol.40 , Issue.1 , pp. 245-256
    • Wei, B.L.1    Brun-Zinkernagel, A.-M.2    Simecka, J.W.3    Pruss, B.M.4    Babitzke, P.5    Romeo, T.6
  • 11
    • 0038349137 scopus 로고    scopus 로고
    • Turnover of FlhD and FlhC, master regulator proteins for Salmonella flagellum biogenesis, by the ATP-dependent ClpXP protease
    • DOI 10.1046/j.1365-2958.2003.03437.x
    • Tomoyasu, T., Takaya, A., Isogai, E. and Yamamoto, T. (2003) Turnover of FlhD and FlhC, master regulator proteins for Salmonella flagellum biogenesis, by the ATP-dependent ClpXP protease. Mol. Microbiol., 48, 443-452. (Pubitemid 36819080)
    • (2003) Molecular Microbiology , vol.48 , Issue.2 , pp. 443-452
    • Tomoyasu, T.1    Takaya, A.2    Isogai, E.3    Yamamoto, T.4
  • 12
    • 33645067394 scopus 로고    scopus 로고
    • The DnaK chaperone machinery converts the native FlhD2C2 hetero-tetramer into a functional transcriptional regulator of flagellar regulon expression in Salmonella
    • Takaya, A., Matsui, M., Tomoyasu, T., Kaya, M. and Yamamoto, T. (2006) The DnaK chaperone machinery converts the native FlhD2C2 hetero-tetramer into a functional transcriptional regulator of flagellar regulon expression in Salmonella. Mol. Microbiol., 59, 1327-1340.
    • (2006) Mol. Microbiol. , vol.59 , pp. 1327-1340
    • Takaya, A.1    Matsui, M.2    Tomoyasu, T.3    Kaya, M.4    Yamamoto, T.5
  • 13
    • 33748763844 scopus 로고    scopus 로고
    • 2 factor in the transcriptional control of the flagellar regulon in Salmonella enterica serovar typhimurium
    • DOI 10.1128/JB.00799-06
    • Yamamoto, S. and Kutsukake, K. (2006) FliT acts as an anti-FlhD2C2 factor in the transcriptional control of the flagellar regulon in Salmonella enterica serovar typhimurium. J. Bacteriol., 188, 6703-6708. (Pubitemid 44412082)
    • (2006) Journal of Bacteriology , vol.188 , Issue.18 , pp. 6703-6708
    • Yamamoto, S.1    Kutsukake, K.2
  • 14
    • 79952804547 scopus 로고    scopus 로고
    • EAL domain protein YdiV acts as an anti-FlhD4C2 factor responsible for nutritional control of the flagellar regulon in Salmonella enterica Serovar Typhimurium
    • Wada, T., Morizane, T., Abo, T., Tominaga, A., Inoue-Tanaka, K. and Kutsukake, K. (2011) EAL domain protein YdiV acts as an anti-FlhD4C2 factor responsible for nutritional control of the flagellar regulon in Salmonella enterica Serovar Typhimurium. J. Bacteriol., 193, 1600-1611.
    • (2011) J. Bacteriol. , vol.193 , pp. 1600-1611
    • Wada, T.1    Morizane, T.2    Abo, T.3    Tominaga, A.4    Inoue-Tanaka, K.5    Kutsukake, K.6
  • 15
    • 77952710839 scopus 로고    scopus 로고
    • Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners
    • Imada, K., Minamino, T., Kinoshita, M., Furukawa, Y. and Namba, K. (2010) Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Proc. Natl Acad. Sci. USA, 107, 8812-8817.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 8812-8817
    • Imada, K.1    Minamino, T.2    Kinoshita, M.3    Furukawa, Y.4    Namba, K.5
  • 16
    • 21844451590 scopus 로고    scopus 로고
    • The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: Enzymatically active and inactive EAL domains
    • DOI 10.1128/JB.187.14.4774-4781.2005
    • Schmidt, A.J., Ryjenkov, D.A. and Gomelsky, M. (2005) The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: enzymatically active and inactive EAL domains. J. Bacteriol., 187, 4774-4781. (Pubitemid 40962195)
    • (2005) Journal of Bacteriology , vol.187 , Issue.14 , pp. 4774-4781
    • Schmidt, A.J.1    Ryjenkov, D.A.2    Gomelsky, M.3
  • 17
    • 25144489145 scopus 로고    scopus 로고
    • The EAL domain protein VieA is a cyclic diguanylate phosphodiesterase
    • DOI 10.1074/jbc.M506500200
    • Tamayo, R., Tischler, A.D. and Camilli, A. (2005) The EAL domain protein VieA is a cyclic diguanylate phosphodiesterase. J. Biol. Chem., 280, 33324-33330. (Pubitemid 41397129)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.39 , pp. 33324-33330
    • Tamayo, R.1    Tischler, A.D.2    Camilli, A.3
  • 18
    • 47049115663 scopus 로고    scopus 로고
    • Catalytic mechanism of cyclic di-GMP-specific phosphodiesterase: a study of the EAL domain-containing RocR from Pseudomonas aeruginosa
    • Rao, F., Yang, Y., Qi, Y. and Liang, Z.X. (2008) Catalytic mechanism of cyclic di-GMP-specific phosphodiesterase: a study of the EAL domain-containing RocR from Pseudomonas aeruginosa. J. Bacteriol., 190, 3622-3631.
    • (2008) J. Bacteriol. , vol.190 , pp. 3622-3631
    • Rao, F.1    Yang, Y.2    Qi, Y.3    Liang, Z.X.4
  • 19
    • 4344688129 scopus 로고    scopus 로고
    • GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessibility to motility
    • DOI 10.1111/j.1365-2958.2004.04206.x
    • Simm, R., Morr, M., Kader, A., Nimtz, M. and Romling, U. (2004) GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessility to motility. Mol. Microbiol., 53, 1123-1134. (Pubitemid 39120434)
    • (2004) Molecular Microbiology , vol.53 , Issue.4 , pp. 1123-1134
    • Simm, R.1    Morr, M.2    Kader, A.3    Nimtz, M.4    Romling, U.5
  • 20
    • 63049137897 scopus 로고    scopus 로고
    • Principles of c-di-GMP signalling in bacteria
    • Hengge, R. (2009) Principles of c-di-GMP signalling in bacteria. Nat. Rev. Microbiol., 7, 263-273.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 263-273
    • Hengge, R.1
  • 21
    • 70349274104 scopus 로고    scopus 로고
    • Structural and mechanistic determinants of c-di-GMP signalling
    • Schirmer, T. and Jenal, U. (2009) Structural and mechanistic determinants of c-di-GMP signalling. Nat. Rev. Microbiol., 7, 724-735.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 724-735
    • Schirmer, T.1    Jenal, U.2
  • 22
    • 67749101868 scopus 로고    scopus 로고
    • Rationalizing the evolution of EAL domain-based cyclic di-GMP-specific phosphodiesterases
    • Romling, U. (2009) Rationalizing the evolution of EAL domain-based cyclic di-GMP-specific phosphodiesterases. J. Bacteriol., 191, 4697-4700.
    • (2009) J. Bacteriol. , vol.191 , pp. 4697-4700
    • Romling, U.1
  • 25
    • 67549109657 scopus 로고    scopus 로고
    • A role for the EAL-like protein STM1344 in regulation of CsgD expression and motility in Salmonella enterica serovar Typhimurium
    • Simm, R., Remminghorst, U., Ahmad, I., Zakikhany, K. and Romling, U. (2009) A role for the EAL-like protein STM1344 in regulation of CsgD expression and motility in Salmonella enterica serovar Typhimurium. J. Bacteriol., 191, 3928-3937.
    • (2009) J. Bacteriol. , vol.191 , pp. 3928-3937
    • Simm, R.1    Remminghorst, U.2    Ahmad, I.3    Zakikhany, K.4    Romling, U.5
  • 26
    • 47049103898 scopus 로고    scopus 로고
    • Multiple genes repress motility in uropathogenic Escherichia coli constitutively expressing type 1 fimbriae
    • Simms, A.N. and Mobley, H.L. (2008) Multiple genes repress motility in uropathogenic Escherichia coli constitutively expressing type 1 fimbriae. J. Bacteriol., 190, 3747-3756.
    • (2008) J. Bacteriol. , vol.190 , pp. 3747-3756
    • Simms, A.N.1    Mobley, H.L.2
  • 27
    • 62649111185 scopus 로고    scopus 로고
    • T-POP array identifies EcnR and PefI-SrgD as novel regulators of flagellar gene expression
    • Wozniak, C.E., Lee, C. and Hughes, K.T. (2009) T-POP array identifies EcnR and PefI-SrgD as novel regulators of flagellar gene expression. J. Bacteriol., 191, 1498-1508.
    • (2009) J. Bacteriol. , vol.191 , pp. 1498-1508
    • Wozniak, C.E.1    Lee, C.2    Hughes, K.T.3
  • 28
    • 34547851781 scopus 로고    scopus 로고
    • Adaptation in bacterial flagellar and motility systems: From regulon members to 'foraging'-like behavior in E. coli
    • DOI 10.1093/nar/gkm456
    • Zhao, K., Liu, M. and Burgess, R.R. (2007) Adaptation in bacterial flagellar and motility systems: from regulon members to 'foraging'-like behavior in E. coli. Nucleic Acids Res., 35, 4441-4452. (Pubitemid 47244595)
    • (2007) Nucleic Acids Research , vol.35 , Issue.13 , pp. 4441-4452
    • Zhao, K.1    Liu, M.2    Burgess, R.R.3
  • 29
    • 84861878881 scopus 로고    scopus 로고
    • Functional and expressional analyses of the anti-FlhD4C2 factor gene ydiV in Escherichia coli
    • Wada, T., Hatamoto, Y. and Kutsukake, K. (2012) Functional and expressional analyses of the anti-FlhD4C2 factor gene ydiV in Escherichia coli. Microbiology, 158, 1533-1542.
    • (2012) Microbiology , vol.158 , pp. 1533-1542
    • Wada, T.1    Hatamoto, Y.2    Kutsukake, K.3
  • 30
    • 51049101679 scopus 로고    scopus 로고
    • An EAL domain protein and cyclic AMP contribute to the interaction between the two quorum sensing systems in Escherichia coli
    • Zhou, X., Meng, X. and Sun, B. (2008) An EAL domain protein and cyclic AMP contribute to the interaction between the two quorum sensing systems in Escherichia coli. Cell Res., 18, 937-948.
    • (2008) Cell Res. , vol.18 , pp. 937-948
    • Zhou, X.1    Meng, X.2    Sun, B.3
  • 31
    • 84855493990 scopus 로고    scopus 로고
    • Regulation of phenotypic heterogeneity permits Salmonella evasion of the host caspase-1 inflammatory response
    • Stewart, M.K., Cummings, L.A., Johnson, M.L., Berezow, A.B. and Cookson, B.T. (2011) Regulation of phenotypic heterogeneity permits Salmonella evasion of the host caspase-1 inflammatory response. Proc. Natl Acad. Sci. USA, 108, 20742-20747.
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 20742-20747
    • Stewart, M.K.1    Cummings, L.A.2    Johnson, M.L.3    Berezow, A.B.4    Cookson, B.T.5
  • 32
    • 84862777801 scopus 로고    scopus 로고
    • YdiV: A dual function protein that targets FlhDC for ClpXP-dependent degradation by promoting release of DNA-bound FlhDC complex
    • Takaya, A., Erhardt, M., Karata, K., Winterberg, K., Yamamoto, T. and Hughes, K.T. (2012) YdiV: a dual function protein that targets FlhDC for ClpXP-dependent degradation by promoting release of DNA-bound FlhDC complex. Mol. Microbiol., 83, 1268-1284.
    • (2012) Mol. Microbiol. , vol.83 , pp. 1268-1284
    • Takaya, A.1    Erhardt, M.2    Karata, K.3    Winterberg, K.4    Yamamoto, T.5    Hughes, K.T.6
  • 33
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Method Enzymol., 276, 307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 39
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • DOI 10.1016/j.jsb.2006.05.009, PII S1047847706001894, Software Tools for Macromolecular Microscopy
    • Tang, G., Peng, L., Baldwin, P.R., Mann, D.S., Jiang, W., Rees, I. and Ludtke, S.J. (2007) EMAN2: an extensible image processing suite for electron microscopy. J. Struct. Biol., 157, 38-46. (Pubitemid 44880785)
    • (2007) Journal of Structural Biology , vol.157 , Issue.1 , pp. 38-46
    • Tang, G.1    Peng, L.2    Baldwin, P.R.3    Mann, D.S.4    Jiang, W.5    Rees, I.6    Ludtke, S.J.7
  • 42
    • 67649746308 scopus 로고    scopus 로고
    • Crystal structures of YkuI and its complex with second messenger cyclic Di-GMP suggest catalytic mechanism of phosphodiester bond cleavage by EAL domains
    • Minasov, G., Padavattan, S., Shuvalova, L., Brunzelle, J.S., Miller, D.J., Basle, A., Massa, C., Collart, F.R., Schirmer, T. and Anderson, W.F. (2009) Crystal structures of YkuI and its complex with second messenger cyclic Di-GMP suggest catalytic mechanism of phosphodiester bond cleavage by EAL domains. J. Biol. Chem., 284, 13174-13184.
    • (2009) J. Biol. Chem. , vol.284 , pp. 13174-13184
    • Minasov, G.1    Padavattan, S.2    Shuvalova, L.3    Brunzelle, J.S.4    Miller, D.J.5    Basle, A.6    Massa, C.7    Collart, F.R.8    Schirmer, T.9    Anderson, W.F.10
  • 43
    • 68149172669 scopus 로고    scopus 로고
    • Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX
    • Navarro, M.V., De, N., Bae, N., Wang, Q. and Sondermann, H. (2009) Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX. Structure, 17, 1104-1116.
    • (2009) Structure , vol.17 , pp. 1104-1116
    • Navarro, M.V.D.N.1    Bae, N.2    Wang, Q.3    Sondermann, H.4
  • 45
    • 0035136267 scopus 로고    scopus 로고
    • Crystal structure of the global regulator FlhD from Escherichia coli at 1.8 A resolution
    • DOI 10.1046/j.1365-2958.2001.02247.x
    • Campos, A., Zhang, R.G., Alkire, R.W., Matsumura, P. and Westbrook, E.M. (2001) Crystal structure of the global regulator FlhD from Escherichia coli at 1.8 A resolution. Mol. Microbiol., 39, 567-580. (Pubitemid 32158138)
    • (2001) Molecular Microbiology , vol.39 , Issue.3 , pp. 567-580
    • Campos, A.1    Zhang, R.2    Alkire, R.W.3    Matsumura, P.4    Westbrook, E.M.5
  • 46
    • 33645894689 scopus 로고    scopus 로고
    • Cyclic di-GMP as a second messenger
    • Romling, U. and Amikam, D. (2006) Cyclic di-GMP as a second messenger. Curr. Opin. Microbiol., 9, 218-228.
    • (2006) Curr. Opin. Microbiol. , vol.9 , pp. 218-228
    • Romling, U.1    Amikam, D.2
  • 47
    • 78049426911 scopus 로고    scopus 로고
    • Comparative genomics of cyclic-di-GMP signalling in bacteria: Post-translational regulation and catalytic activity
    • Seshasayee, A.S., Fraser, G.M. and Luscombe, N.M. (2010) Comparative genomics of cyclic-di-GMP signalling in bacteria: post-translational regulation and catalytic activity. Nucleic Acids Res., 38, 5970-5981.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 5970-5981
    • Seshasayee, A.S.1    Fraser, G.M.2    Luscombe, N.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.