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Volumn 59, Issue 1, 2015, Pages 104-116

A Phosphosignaling Adaptor Primes the AAA+ Protease ClpXP to Drive Cell Cycle-Regulated Proteolysis

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; ATPASES ASSOCIATED WITH DIVERSE CELLULAR ACTIVITIES PROTEASE; PROTEASE CLPXP; PROTEINASE; PROTEOME; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATASE; BACTERIAL PROTEIN; ENDOPEPTIDASE CLP; PROTEIN BINDING;

EID: 84937163099     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2015.05.014     Document Type: Article
Times cited : (39)

References (49)
  • 1
    • 80051726238 scopus 로고    scopus 로고
    • Regulatory cohesion of cell cycle and cell differentiation through interlinked phosphorylation and second messenger networks
    • Abel S., Chien P., Wassmann P., Schirmer T., Kaever V., Laub M.T., Baker T.A., Jenal U. Regulatory cohesion of cell cycle and cell differentiation through interlinked phosphorylation and second messenger networks. Mol. Cell 2011, 43:550-560.
    • (2011) Mol. Cell , vol.43 , pp. 550-560
    • Abel, S.1    Chien, P.2    Wassmann, P.3    Schirmer, T.4    Kaever, V.5    Laub, M.T.6    Baker, T.A.7    Jenal, U.8
  • 2
    • 0026009504 scopus 로고
    • Genetic analysis of a temporally transcribed chemotaxis gene cluster in Caulobacter crescentus
    • Alley M.R.K., Gomes S.L., Alexander W., Shapiro L. Genetic analysis of a temporally transcribed chemotaxis gene cluster in Caulobacter crescentus. Genetics 1991, 129:333-341.
    • (1991) Genetics , vol.129 , pp. 333-341
    • Alley, M.R.K.1    Gomes, S.L.2    Alexander, W.3    Shapiro, L.4
  • 3
    • 0027409274 scopus 로고
    • Requirement of the carboxyl terminus of a bacterial chemoreceptor for its targeted proteolysis
    • Alley M.R., Maddock J.R., Shapiro L. Requirement of the carboxyl terminus of a bacterial chemoreceptor for its targeted proteolysis. Science 1993, 259:1754-1757.
    • (1993) Science , vol.259 , pp. 1754-1757
    • Alley, M.R.1    Maddock, J.R.2    Shapiro, L.3
  • 4
    • 84877081415 scopus 로고    scopus 로고
    • Roles of adaptor proteins in regulation of bacterial proteolysis
    • Battesti A., Gottesman S. Roles of adaptor proteins in regulation of bacterial proteolysis. Curr. Opin. Microbiol. 2013, 16:140-147.
    • (2013) Curr. Opin. Microbiol. , vol.16 , pp. 140-147
    • Battesti, A.1    Gottesman, S.2
  • 5
    • 84879014705 scopus 로고    scopus 로고
    • Identification of ClpP substrates in Caulobacter crescentus reveals a role for regulated proteolysis in bacterial development
    • Bhat N.H., Vass R.H., Stoddard P.R., Shin D.K., Chien P. Identification of ClpP substrates in Caulobacter crescentus reveals a role for regulated proteolysis in bacterial development. Mol. Microbiol. 2013, 88:1083-1092.
    • (2013) Mol. Microbiol. , vol.88 , pp. 1083-1092
    • Bhat, N.H.1    Vass, R.H.2    Stoddard, P.R.3    Shin, D.K.4    Chien, P.5
  • 7
    • 1242271992 scopus 로고    scopus 로고
    • Bivalent tethering of SspB to ClpXP is required for efficient substrate delivery: a protein-design study
    • Bolon D.N., Wah D.A., Hersch G.L., Baker T.A., Sauer R.T. Bivalent tethering of SspB to ClpXP is required for efficient substrate delivery: a protein-design study. Mol. Cell 2004, 13:443-449.
    • (2004) Mol. Cell , vol.13 , pp. 443-449
    • Bolon, D.N.1    Wah, D.A.2    Hersch, G.L.3    Baker, T.A.4    Sauer, R.T.5
  • 8
    • 77949880884 scopus 로고    scopus 로고
    • Receiver domain structure and function in response regulator proteins
    • Bourret R.B. Receiver domain structure and function in response regulator proteins. Curr. Opin. Microbiol. 2010, 13:142-149.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 142-149
    • Bourret, R.B.1
  • 9
    • 72449175369 scopus 로고    scopus 로고
    • Dynamics of two Phosphorelays controlling cell cycle progression in Caulobacter crescentus
    • Chen Y.E., Tsokos C.G., Biondi E.G., Perchuk B.S., Laub M.T. Dynamics of two Phosphorelays controlling cell cycle progression in Caulobacter crescentus. J.Bacteriol. 2009, 191:7417-7429.
    • (2009) J.Bacteriol. , vol.191 , pp. 7417-7429
    • Chen, Y.E.1    Tsokos, C.G.2    Biondi, E.G.3    Perchuk, B.S.4    Laub, M.T.5
  • 11
    • 41249085227 scopus 로고    scopus 로고
    • The flexible attachment of the N-domains to the ClpA ring body allows their use on demand
    • Cranz-Mileva S., Imkamp F., Kolygo K., Maglica Z., Kress W., Weber-Ban E. The flexible attachment of the N-domains to the ClpA ring body allows their use on demand. J.Mol. Biol. 2008, 378:412-424.
    • (2008) J.Mol. Biol. , vol.378 , pp. 412-424
    • Cranz-Mileva, S.1    Imkamp, F.2    Kolygo, K.3    Maglica, Z.4    Kress, W.5    Weber-Ban, E.6
  • 12
    • 69249134629 scopus 로고    scopus 로고
    • Engineering synthetic adaptors and substrates for controlled ClpXP degradation
    • Davis J.H., Baker T.A., Sauer R.T. Engineering synthetic adaptors and substrates for controlled ClpXP degradation. J.Biol. Chem. 2009, 284:21848-21855.
    • (2009) J.Biol. Chem. , vol.284 , pp. 21848-21855
    • Davis, J.H.1    Baker, T.A.2    Sauer, R.T.3
  • 13
    • 0015505531 scopus 로고
    • Chromosome replication during development in Caulobacter crescentus
    • Degnen S.T., Newton A. Chromosome replication during development in Caulobacter crescentus. J.Mol. Biol. 1972, 64:671-680.
    • (1972) J.Mol. Biol. , vol.64 , pp. 671-680
    • Degnen, S.T.1    Newton, A.2
  • 14
    • 0036210995 scopus 로고    scopus 로고
    • ClpS, a substrate modulator of the ClpAP machine
    • Dougan D.A., Reid B.G., Horwich A.L., Bukau B. ClpS, a substrate modulator of the ClpAP machine. Mol. Cell 2002, 9:673-683.
    • (2002) Mol. Cell , vol.9 , pp. 673-683
    • Dougan, D.A.1    Reid, B.G.2    Horwich, A.L.3    Bukau, B.4
  • 15
    • 0141957392 scopus 로고    scopus 로고
    • Targeted delivery of an ssrA-tagged substrate by the adaptor protein SspB to its cognate AAA+ protein ClpX
    • Dougan D.A., Weber-Ban E., Bukau B. Targeted delivery of an ssrA-tagged substrate by the adaptor protein SspB to its cognate AAA+ protein ClpX. Mol. Cell 2003, 12:373-380.
    • (2003) Mol. Cell , vol.12 , pp. 373-380
    • Dougan, D.A.1    Weber-Ban, E.2    Bukau, B.3
  • 16
    • 58149485506 scopus 로고    scopus 로고
    • Second messenger-mediated spatiotemporal control of protein degradation regulates bacterial cell cycle progression
    • Duerig A., Abel S., Folcher M., Nicollier M., Schwede T., Amiot N., Giese B., Jenal U. Second messenger-mediated spatiotemporal control of protein degradation regulates bacterial cell cycle progression. Genes Dev. 2009, 23:93-104.
    • (2009) Genes Dev. , vol.23 , pp. 93-104
    • Duerig, A.1    Abel, S.2    Folcher, M.3    Nicollier, M.4    Schwede, T.5    Amiot, N.6    Giese, B.7    Jenal, U.8
  • 18
    • 77949887724 scopus 로고    scopus 로고
    • Molecular strategies for phosphorylation-mediated regulation of response regulator activity
    • Gao R., Stock A.M. Molecular strategies for phosphorylation-mediated regulation of response regulator activity. Curr. Opin. Microbiol. 2010, 13:160-167.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 160-167
    • Gao, R.1    Stock, A.M.2
  • 19
    • 79955770162 scopus 로고    scopus 로고
    • Scaffold proteins: hubs for controlling the flow of cellular information
    • Good M.C., Zalatan J.G., Lim W.A. Scaffold proteins: hubs for controlling the flow of cellular information. Science 2011, 332:680-686.
    • (2011) Science , vol.332 , pp. 680-686
    • Good, M.C.1    Zalatan, J.G.2    Lim, W.A.3
  • 20
    • 0032524297 scopus 로고    scopus 로고
    • Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP
    • Grimaud R., Kessel M., Beuron F., Steven A.C., Maurizi M.R. Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP. J.Biol. Chem. 1998, 273:12476-12481.
    • (1998) J.Biol. Chem. , vol.273 , pp. 12476-12481
    • Grimaud, R.1    Kessel, M.2    Beuron, F.3    Steven, A.C.4    Maurizi, M.R.5
  • 21
    • 71749093772 scopus 로고    scopus 로고
    • Proteolysis of sigmaS (RpoS) and the general stress response in Escherichia coli
    • Hengge R. Proteolysis of sigmaS (RpoS) and the general stress response in Escherichia coli. Res. Microbiol. 2009, 160:667-676.
    • (2009) Res. Microbiol. , vol.160 , pp. 667-676
    • Hengge, R.1
  • 22
    • 55949128346 scopus 로고    scopus 로고
    • A bacterial control circuit integrates polar localization and proteolysis of key regulatory proteins with a phospho-signaling cascade
    • Iniesta A.A., Shapiro L. A bacterial control circuit integrates polar localization and proteolysis of key regulatory proteins with a phospho-signaling cascade. Proc. Natl. Acad. Sci. USA 2008, 105:16602-16607.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 16602-16607
    • Iniesta, A.A.1    Shapiro, L.2
  • 23
    • 33746610535 scopus 로고    scopus 로고
    • A phospho-signaling pathway controls the localization and activity of a protease complex critical for bacterial cell cycle progression
    • Iniesta A.A., McGrath P.T., Reisenauer A., McAdams H.H., Shapiro L. A phospho-signaling pathway controls the localization and activity of a protease complex critical for bacterial cell cycle progression. Proc. Natl. Acad. Sci. USA 2006, 103:10935-10940.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 10935-10940
    • Iniesta, A.A.1    McGrath, P.T.2    Reisenauer, A.3    McAdams, H.H.4    Shapiro, L.5
  • 24
    • 71749085978 scopus 로고    scopus 로고
    • The role of proteolysis in the Caulobacter crescentus cell cycle and development
    • Jenal U. The role of proteolysis in the Caulobacter crescentus cell cycle and development. Res. Microbiol. 2009, 160:687-695.
    • (2009) Res. Microbiol. , vol.160 , pp. 687-695
    • Jenal, U.1
  • 25
    • 0032189273 scopus 로고    scopus 로고
    • An essential protease involved in bacterial cell-cycle control
    • Jenal U., Fuchs T. An essential protease involved in bacterial cell-cycle control. EMBO J. 1998, 17:5658-5669.
    • (1998) EMBO J. , vol.17 , pp. 5658-5669
    • Jenal, U.1    Fuchs, T.2
  • 26
    • 0032510783 scopus 로고    scopus 로고
    • A bacterial two-hybrid system based on a reconstituted signal transduction pathway
    • Karimova G., Pidoux J., Ullmann A., Ladant D. A bacterial two-hybrid system based on a reconstituted signal transduction pathway. Proc. Natl. Acad. Sci. USA 1998, 95:5752-5756.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5752-5756
    • Karimova, G.1    Pidoux, J.2    Ullmann, A.3    Ladant, D.4
  • 27
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: a case study using the Phyre server
    • Kelley L.A., Sternberg M.J.E. Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protoc. 2009, 4:363-371.
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.E.2
  • 30
    • 67651208925 scopus 로고    scopus 로고
    • Adapting the machine: adaptor proteins for Hsp100/Clp and AAA+ proteases
    • Kirstein J., Molière N., Dougan D.A., Turgay K. Adapting the machine: adaptor proteins for Hsp100/Clp and AAA+ proteases. Nat. Rev. Microbiol. 2009, 7:589-599.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 589-599
    • Kirstein, J.1    Molière, N.2    Dougan, D.A.3    Turgay, K.4
  • 31
    • 70350154538 scopus 로고    scopus 로고
    • Sinorhizobium meliloti CpdR1 is critical for co-ordinating cell cycle progression and the symbiotic chronic infection
    • Kobayashi H., De Nisco N.J., Chien P., Simmons L.A., Walker G.C. Sinorhizobium meliloti CpdR1 is critical for co-ordinating cell cycle progression and the symbiotic chronic infection. Mol. Microbiol. 2009, 73:586-600.
    • (2009) Mol. Microbiol. , vol.73 , pp. 586-600
    • Kobayashi, H.1    De Nisco, N.J.2    Chien, P.3    Simmons, L.A.4    Walker, G.C.5
  • 32
    • 0034730496 scopus 로고    scopus 로고
    • A specificity-enhancing factor for the ClpXP degradation machine
    • Levchenko I., Seidel M., Sauer R.T., Baker T.A. A specificity-enhancing factor for the ClpXP degradation machine. Science 2000, 289:2354-2356.
    • (2000) Science , vol.289 , pp. 2354-2356
    • Levchenko, I.1    Seidel, M.2    Sauer, R.T.3    Baker, T.A.4
  • 33
    • 0141992126 scopus 로고    scopus 로고
    • Structure of a delivery protein for an AAA+ protease in complex with a peptide degradation tag
    • Levchenko I., Grant R.A., Wah D.A., Sauer R.T., Baker T.A. Structure of a delivery protein for an AAA+ protease in complex with a peptide degradation tag. Mol. Cell 2003, 12:365-372.
    • (2003) Mol. Cell , vol.12 , pp. 365-372
    • Levchenko, I.1    Grant, R.A.2    Wah, D.A.3    Sauer, R.T.4    Baker, T.A.5
  • 34
    • 0035107305 scopus 로고    scopus 로고
    • Characterization of the N-terminal repeat domain of Escherichia coli ClpA-A class I Clp/HSP100 ATPase
    • Lo J.H., Baker T.A., Sauer R.T. Characterization of the N-terminal repeat domain of Escherichia coli ClpA-A class I Clp/HSP100 ATPase. Protein Sci. 2001, 10:551-559.
    • (2001) Protein Sci. , vol.10 , pp. 551-559
    • Lo, J.H.1    Baker, T.A.2    Sauer, R.T.3
  • 35
    • 32044454838 scopus 로고    scopus 로고
    • A dynamically localized protease complex and a polar specificity factor control a cell cycle master regulator
    • McGrath P.T., Iniesta A.A., Ryan K.R., Shapiro L., McAdams H.H. A dynamically localized protease complex and a polar specificity factor control a cell cycle master regulator. Cell 2006, 124:535-547.
    • (2006) Cell , vol.124 , pp. 535-547
    • McGrath, P.T.1    Iniesta, A.A.2    Ryan, K.R.3    Shapiro, L.4    McAdams, H.H.5
  • 36
    • 33847108004 scopus 로고    scopus 로고
    • Structural basis of SspB-tail recognition by the zinc binding domain of ClpX
    • Park E.Y., Lee B.-G., Hong S.-B., Kim H.-W., Jeon H., Song H.K. Structural basis of SspB-tail recognition by the zinc binding domain of ClpX. J.Mol. Biol. 2007, 367:514-526.
    • (2007) J.Mol. Biol. , vol.367 , pp. 514-526
    • Park, E.Y.1    Lee, B.-G.2    Hong, S.-B.3    Kim, H.-W.4    Jeon, H.5    Song, H.K.6
  • 37
    • 0031940593 scopus 로고    scopus 로고
    • Negative control of bacterial DNA replication by a cell cycle regulatory protein that binds at the chromosome origin
    • Quon K.C., Yang B., Domian I.J., Shapiro L., Marczynski G.T. Negative control of bacterial DNA replication by a cell cycle regulatory protein that binds at the chromosome origin. Proc. Natl. Acad. Sci. USA 1998, 95:120-125.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 120-125
    • Quon, K.C.1    Yang, B.2    Domian, I.J.3    Shapiro, L.4    Marczynski, G.T.5
  • 38
    • 74049141363 scopus 로고    scopus 로고
    • Coupling prokaryotic cell fate and division control with a bifunctional and oscillating oxidoreductase homolog
    • Radhakrishnan S.K., Pritchard S., Viollier P.H. Coupling prokaryotic cell fate and division control with a bifunctional and oscillating oxidoreductase homolog. Dev. Cell 2010, 18:90-101.
    • (2010) Dev. Cell , vol.18 , pp. 90-101
    • Radhakrishnan, S.K.1    Pritchard, S.2    Viollier, P.H.3
  • 39
    • 84863533607 scopus 로고    scopus 로고
    • Adaptor-dependent degradation of a cell-cycle regulator uses a unique substrate architecture
    • Rood K.L., Clark N.E., Stoddard P.R., Garman S.C., Chien P. Adaptor-dependent degradation of a cell-cycle regulator uses a unique substrate architecture. Structure 2012, 20:1223-1232.
    • (2012) Structure , vol.20 , pp. 1223-1232
    • Rood, K.L.1    Clark, N.E.2    Stoddard, P.R.3    Garman, S.C.4    Chien, P.5
  • 40
    • 84911431183 scopus 로고    scopus 로고
    • FliT selectively enhances proteolysis of FlhC subunit in FlhD4C2 complex by an ATP-dependent protease, ClpXP
    • Sato Y., Takaya A., Mouslim C., Hughes K.T., Yamamoto T. FliT selectively enhances proteolysis of FlhC subunit in FlhD4C2 complex by an ATP-dependent protease, ClpXP. J.Biol. Chem. 2014, 289:33001-33011.
    • (2014) J.Biol. Chem. , vol.289 , pp. 33001-33011
    • Sato, Y.1    Takaya, A.2    Mouslim, C.3    Hughes, K.T.4    Yamamoto, T.5
  • 42
    • 26444481955 scopus 로고    scopus 로고
    • Two-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: a system-level analysis
    • Skerker J.M., Prasol M.S., Perchuk B.S., Biondi E.G., Laub M.T. Two-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: a system-level analysis. PLoS Biol. 2005, 3:e334.
    • (2005) PLoS Biol. , vol.3
    • Skerker, J.M.1    Prasol, M.S.2    Perchuk, B.S.3    Biondi, E.G.4    Laub, M.T.5
  • 43
    • 84907584965 scopus 로고    scopus 로고
    • Cell cycle-dependent adaptor complex for ClpXP-mediated proteolysis directly integrates phosphorylation and second messenger signals
    • Smith S.C., Joshi K.K., Zik J.J., Trinh K., Kamajaya A., Chien P., Ryan K.R. Cell cycle-dependent adaptor complex for ClpXP-mediated proteolysis directly integrates phosphorylation and second messenger signals. Proc. Natl. Acad. Sci. USA 2014, 111:14229-14234.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 14229-14234
    • Smith, S.C.1    Joshi, K.K.2    Zik, J.J.3    Trinh, K.4    Kamajaya, A.5    Chien, P.6    Ryan, K.R.7
  • 44
    • 0041465001 scopus 로고    scopus 로고
    • Sequential recognition of two distinct sites in sigma(S) by the proteolytic targeting factor RssB and ClpX
    • Stüdemann A., Noirclerc-Savoye M., Klauck E., Becker G., Schneider D., Hengge R. Sequential recognition of two distinct sites in sigma(S) by the proteolytic targeting factor RssB and ClpX. EMBO J. 2003, 22:4111-4120.
    • (2003) EMBO J. , vol.22 , pp. 4111-4120
    • Stüdemann, A.1    Noirclerc-Savoye, M.2    Klauck, E.3    Becker, G.4    Schneider, D.5    Hengge, R.6
  • 45
    • 70350196362 scopus 로고    scopus 로고
    • Mutations that alter RcdA surface residues decouple protein localization and CtrA proteolysis in Caulobacter crescentus
    • Taylor J.A., Wilbur J.D., Smith S.C., Ryan K.R. Mutations that alter RcdA surface residues decouple protein localization and CtrA proteolysis in Caulobacter crescentus. J.Mol. Biol. 2009, 394:46-60.
    • (2009) J.Mol. Biol. , vol.394 , pp. 46-60
    • Taylor, J.A.1    Wilbur, J.D.2    Smith, S.C.3    Ryan, K.R.4
  • 46
    • 84872272882 scopus 로고    scopus 로고
    • Polarity and cell fate asymmetry in Caulobacter crescentus
    • Tsokos C.G., Laub M.T. Polarity and cell fate asymmetry in Caulobacter crescentus. Curr. Opin. Microbiol. 2012, 15:744-750.
    • (2012) Curr. Opin. Microbiol. , vol.15 , pp. 744-750
    • Tsokos, C.G.1    Laub, M.T.2
  • 47
    • 0036848756 scopus 로고    scopus 로고
    • Characterization of a specificity factor for an AAA+ ATPase: assembly of SspB dimers withssrA-tagged proteins and the ClpX hexamer
    • Wah D.A., Levchenko I., Baker T.A., Sauer R.T. Characterization of a specificity factor for an AAA+ ATPase: assembly of SspB dimers withssrA-tagged proteins and the ClpX hexamer. Chem. Biol. 2002, 9:1237-1245.
    • (2002) Chem. Biol. , vol.9 , pp. 1237-1245
    • Wah, D.A.1    Levchenko, I.2    Baker, T.A.3    Sauer, R.T.4
  • 48
    • 0141888401 scopus 로고    scopus 로고
    • Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease
    • Wah D.A., Levchenko I., Rieckhof G.E., Bolon D.N., Baker T.A., Sauer R.T. Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease. Mol. Cell 2003, 12:355-363.
    • (2003) Mol. Cell , vol.12 , pp. 355-363
    • Wah, D.A.1    Levchenko, I.2    Rieckhof, G.E.3    Bolon, D.N.4    Baker, T.A.5    Sauer, R.T.6
  • 49
    • 0035281566 scopus 로고    scopus 로고
    • The RssB response regulator directly targets sigma(S) for degradation by ClpXP
    • Zhou Y., Gottesman S., Hoskins J.R., Maurizi M.R., Wickner S. The RssB response regulator directly targets sigma(S) for degradation by ClpXP. Genes Dev. 2001, 15:627-637.
    • (2001) Genes Dev. , vol.15 , pp. 627-637
    • Zhou, Y.1    Gottesman, S.2    Hoskins, J.R.3    Maurizi, M.R.4    Wickner, S.5


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