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Volumn 193, Issue 8, 2011, Pages 1911-1918

The Interplay of ClpXP with the cell division machinery in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

CLPXP PROTEIN; FTSZ PROTEIN; PROTEINASE; UNCLASSIFIED DRUG;

EID: 79955460424     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01317-10     Document Type: Article
Times cited : (44)

References (40)
  • 1
    • 69249126551 scopus 로고    scopus 로고
    • Bacterial cell division: assembly, maintenance and disassembly of the Z ring
    • Adams, D. W., and J. Errington. 2009. Bacterial cell division: assembly, maintenance and disassembly of the Z ring. Nat. Rev. Microbiol. 7:642-653.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 642-653
    • Adams, D.W.1    Errington, J.2
  • 2
    • 0026757024 scopus 로고
    • Cell division in Escherichia coli minB mutants
    • Akerlund, T., R. Bernander, and K. Nordstrom. 1992. Cell division in Escherichia coli minB mutants. Mol. Microbiol. 6:2073-2083.
    • (1992) Mol. Microbiol. , vol.6 , pp. 2073-2083
    • Akerlund, T.1    Bernander, R.2    Nordstrom, K.3
  • 4
    • 4344652693 scopus 로고    scopus 로고
    • Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins
    • Anderson, D. E., F. J. Gueiros-Filho, and H. P. Erickson. 2004. Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins. J. Bacteriol. 186:5775-5781.
    • (2004) J. Bacteriol. , vol.186 , pp. 5775-5781
    • Anderson, D.E.1    Gueiros-Filho, F.J.2    Erickson, H.P.3
  • 5
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, singlegene knockout mutants: the Keio collection
    • Baba, T., et al. 2006. Construction of Escherichia coli K-12 in-frame, singlegene knockout mutants: the Keio collection. Mol. Syst. Biol. 2:2006.0008.
    • (2006) Mol. Syst. Biol. , vol.2 , Issue.2006 , pp. 0008
    • Baba, T.1
  • 6
    • 39749142159 scopus 로고    scopus 로고
    • Conditional lethality, division defects, membrane involution, and endocytosis in mre and mrd shape mutants of Escherichia coli
    • Bendezu, F. O., and P. A. de Boer. 2008. Conditional lethality, division defects, membrane involution, and endocytosis in mre and mrd shape mutants of Escherichia coli. J. Bacteriol. 190:1792-1811.
    • (2008) J. Bacteriol. , vol.190 , pp. 1792-1811
    • Bendezu, F.O.1    de Boer, P.A.2
  • 7
    • 2942538589 scopus 로고    scopus 로고
    • Screening for synthetic lethal mutants in Escherichia coli and identification of EnvC (YibP) as a periplasmic septal ring factor with murein hydrolase activity
    • Bernhardt, T. G., and P. A. de Boer. 2004. Screening for synthetic lethal mutants in Escherichia coli and identification of EnvC (YibP) as a periplasmic septal ring factor with murein hydrolase activity. Mol. Microbiol. 52: 1255-1269.
    • (2004) Mol. Microbiol. , vol.52 , pp. 1255-1269
    • Bernhardt, T.G.1    de Boer, P.A.2
  • 8
    • 19444386428 scopus 로고    scopus 로고
    • SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over chromosomes in E. coli.
    • Bernhardt, T. G., and P. A. de Boer. 2005. SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over chromosomes in E. coli. Mol. Cell 18:555-564.
    • (2005) Mol. Cell , vol.18 , pp. 555-564
    • Bernhardt, T.G.1    de Boer, P.A.2
  • 9
    • 0024991124 scopus 로고
    • Analysis of ftsZ mutations that confer resistance to the cell division inhibitor SulA (SfiA)
    • Bi, E., and J. Lutkenhaus. 1990. Analysis of ftsZ mutations that confer resistance to the cell division inhibitor SulA (SfiA). J. Bacteriol. 172:5602-5609.
    • (1990) J. Bacteriol. , vol.172 , pp. 5602-5609
    • Bi, E.1    Lutkenhaus, J.2
  • 10
    • 15444350252 scopus 로고    scopus 로고
    • The complete genome sequence of Escherichia coli K-12
    • Blattner, F. R., et al. 1997. The complete genome sequence of Escherichia coli K-12. Science 277:1453-1462.
    • (1997) Science , vol.277 , pp. 1453-1462
    • Blattner, F.R.1
  • 11
    • 67649811066 scopus 로고    scopus 로고
    • ClpXP protease degrades the cytoskeletal protein, FtsZ, and modulates FtsZ polymer dynamics
    • Camberg, J. L., J. R. Hoskins, and S. Wickner. 2009. ClpXP protease degrades the cytoskeletal protein, FtsZ, and modulates FtsZ polymer dynamics. Proc. Natl. Acad. Sci. U. S. A. 106:10614-10619.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 10614-10619
    • Camberg, J.L.1    Hoskins, J.R.2    Wickner, S.3
  • 12
    • 20444457941 scopus 로고    scopus 로고
    • Rapid in vitro assembly dynamics and subunit turnover of FtsZ demonstrated by fluorescence resonance energy transfer
    • Chen, Y., and H. P. Erickson. 2005. Rapid in vitro assembly dynamics and subunit turnover of FtsZ demonstrated by fluorescence resonance energy transfer. J. Biol. Chem. 280:22549-22554.
    • (2005) J. Biol. Chem. , vol.280 , pp. 22549-22554
    • Chen, Y.1    Erickson, H.P.2
  • 13
    • 0029065955 scopus 로고
    • Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant
    • Cherepanov, P. P., and W. Wackernagel. 1995. Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant. Gene 158:9-14.
    • (1995) Gene , vol.158 , pp. 9-14
    • Cherepanov, P.P.1    Wackernagel, W.2
  • 14
    • 0026697767 scopus 로고
    • The proper ratio of FtsZ to FtsA is required for cell division to occur in Escherichia coli
    • Dai, K., and J. Lutkenhaus. 1992. The proper ratio of FtsZ to FtsA is required for cell division to occur in Escherichia coli. J. Bacteriol. 174:6145-6151.
    • (1992) J. Bacteriol. , vol.174 , pp. 6145-6151
    • Dai, K.1    Lutkenhaus, J.2
  • 15
    • 0027167446 scopus 로고
    • Cloning and characterization of ftsN, an essential cell division gene in Escherichia coli isolated as a multicopy suppressor of ftsA12(Ts)
    • Dai, K., Y. Xu, and J. Lutkenhaus. 1993. Cloning and characterization of ftsN, an essential cell division gene in Escherichia coli isolated as a multicopy suppressor of ftsA12(Ts). J. Bacteriol. 175:3790-3797.
    • (1993) J. Bacteriol. , vol.175 , pp. 3790-3797
    • Dai, K.1    Xu, Y.2    Lutkenhaus, J.3
  • 16
    • 39249085850 scopus 로고    scopus 로고
    • MinC spatially controls bacterial cytokinesis by antagonizing the scaffolding function of FtsZ
    • Dajkovic, A., G. Lan, S. X. Sun, D. Wirtz, and J. Lutkenhaus. 2008. MinC spatially controls bacterial cytokinesis by antagonizing the scaffolding function of FtsZ. Curr. Biol. 18:235-244.
    • (2008) Curr. Biol. , vol.18 , pp. 235-244
    • Dajkovic, A.1    Lan, G.2    Sun, S.X.3    Wirtz, D.4    Lutkenhaus, J.5
  • 17
    • 0024977391 scopus 로고
    • A division inhibitor and a topological specificity factor coded for by the minicell locus determine proper placement of the division septum in E. coli
    • de Boer, P. A., R. E. Crossley, and L. I. Rothfield. 1989. A division inhibitor and a topological specificity factor coded for by the minicell locus determine proper placement of the division septum in E. coli. Cell 56:641-649.
    • (1989) Cell , vol.56 , pp. 641-649
    • de Boer, P.A.1    Crossley, R.E.2    Rothfield, L.I.3
  • 18
    • 77955374003 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis ClpX interacts with FtsZ and interferes with FtsZ assembly
    • Dziedzic, R., et al. 2010. Mycobacterium tuberculosis ClpX interacts with FtsZ and interferes with FtsZ assembly. PLoS One 5:e11058.
    • (2010) PLoS One , vol.5
    • Dziedzic, R.1
  • 19
    • 0037351068 scopus 로고    scopus 로고
    • Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals
    • Flynn, J. M., S. B. Neher, Y. I. Kim, R. T. Sauer, and T. A. Baker. 2003. Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals. Mol. Cell 11:671-683.
    • (2003) Mol. Cell , vol.11 , pp. 671-683
    • Flynn, J.M.1    Neher, S.B.2    Kim, Y.I.3    Sauer, R.T.4    Baker, T.A.5
  • 20
    • 0027364289 scopus 로고
    • ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities.
    • Gottesman, S., W. P. Clark, V. de Crecy-Lagard, and M. R. Maurizi. 1993. ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities. J. Biol. Chem. 268:22618-22626.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22618-22626
    • Gottesman, S.1    Clark, W.P.2    de Crecy-Lagard, V.3    Maurizi, M.R.4
  • 22
    • 63049127158 scopus 로고    scopus 로고
    • ClpX inhibits FtsZ assembly in a manner that does not require its ATP hydrolysis-dependent chaperone activity
    • Haeusser, D. P., A. H. Lee, R. B. Weart, and P. A. Levin. 2009. ClpX inhibits FtsZ assembly in a manner that does not require its ATP hydrolysis-dependent chaperone activity. J. Bacteriol. 191:1986-1991.
    • (2009) J. Bacteriol. , vol.191 , pp. 1986-1991
    • Haeusser, D.P.1    Lee, A.H.2    Weart, R.B.3    Levin, P.A.4
  • 23
    • 21244482459 scopus 로고    scopus 로고
    • Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: allosteric control of a protein machine
    • Hersch, G. L., R. E. Burton, D. N. Bolon, T. A. Baker, and R. T. Sauer. 2005. Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: allosteric control of a protein machine. Cell 121:1017-1027.
    • (2005) Cell , vol.121 , pp. 1017-1027
    • Hersch, G.L.1    Burton, R.E.2    Bolon, D.N.3    Baker, T.A.4    Sauer, R.T.5
  • 24
    • 0034255124 scopus 로고    scopus 로고
    • Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP
    • Hoskins, J. R., S. K. Singh, M. R. Maurizi, and S. Wickner. 2000. Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP. Proc. Natl. Acad. Sci. U. S. A. 97:8892-8897.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 8892-8897
    • Hoskins, J.R.1    Singh, S.K.2    Maurizi, M.R.3    Wickner, S.4
  • 25
    • 0034964370 scopus 로고    scopus 로고
    • Topological regulation of cell division in E. coli. Spatiotemporal oscillation of MinD requires stimulation of its ATPase by MinE and phospholipid
    • Hu, Z., and J. Lutkenhaus. 2001. Topological regulation of cell division in E. coli. Spatiotemporal oscillation of MinD requires stimulation of its ATPase by MinE and phospholipid. Mol. Cell 7:1337-1343.
    • (2001) Mol. Cell , vol.7 , pp. 1337-1343
    • Hu, Z.1    Lutkenhaus, J.2
  • 26
    • 77952352778 scopus 로고    scopus 로고
    • Multiple modes of interconverting dynamic pattern formation by bacterial cell division proteins
    • Ivanov, V., and K. Mizuuchi. 2010. Multiple modes of interconverting dynamic pattern formation by bacterial cell division proteins. Proc. Natl. Acad. Sci. U. S. A. 107:8071-8078.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 8071-8078
    • Ivanov, V.1    Mizuuchi, K.2
  • 27
    • 36248938686 scopus 로고    scopus 로고
    • The structure of FtsZ filaments in vivo suggests a force-generating role in cell division
    • Li, Z., M. J. Trimble, Y. V. Brun, and G. J. Jensen. 2007. The structure of FtsZ filaments in vivo suggests a force-generating role in cell division. EMBO J. 26:4694-4708.
    • (2007) EMBO J , vol.26 , pp. 4694-4708
    • Li, Z.1    Trimble, M.J.2    Brun, Y.V.3    Jensen, G.J.4
  • 28
    • 34548630230 scopus 로고    scopus 로고
    • Assembly dynamics of the bacterial MinCDE system and spatial regulation of the Z ring
    • Lutkenhaus, J. 2007. Assembly dynamics of the bacterial MinCDE system and spatial regulation of the Z ring. Annu. Rev. Biochem. 76:539-562.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 539-562
    • Lutkenhaus, J.1
  • 29
    • 0035807879 scopus 로고    scopus 로고
    • Pattern formation in Escherichiacoli: a model for the pole-to-pole oscillations of Min proteins and the localization of the division site
    • Meinhardt, H., and P. A. de Boer. 2001. Pattern formation in Escherichiacoli: a model for the pole-to-pole oscillations of Min proteins and the localization of the division site. Proc. Natl. Acad. Sci. U. S. A. 98:14202-14207.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 14202-14207
    • Meinhardt, H.1    de Boer, P.A.2
  • 30
    • 33646021005 scopus 로고    scopus 로고
    • Proteomic profiling of ClpXP substrates after DNA damage reveals extensive instability within SOS regulon
    • Neher, S. B., et al. 2006. Proteomic profiling of ClpXP substrates after DNA damage reveals extensive instability within SOS regulon. Mol. Cell 22:193-204.
    • (2006) Mol. Cell , vol.22 , pp. 193-204
    • Neher, S.B.1
  • 31
    • 38349097870 scopus 로고    scopus 로고
    • Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin
    • Roll-Mecak, A., and R. D. Vale. 2008. Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin. Nature 451:363-367.
    • (2008) Nature , vol.451 , pp. 363-367
    • Roll-Mecak, A.1    Vale, R.D.2
  • 32
    • 5344269437 scopus 로고    scopus 로고
    • Sculpting the proteome with AAA(+) proteases and disassembly machines
    • Sauer, R. T., et al. 2004. Sculpting the proteome with AAA(+) proteases and disassembly machines. Cell 119:9-18.
    • (2004) Cell , vol.119 , pp. 9-18
    • Sauer, R.T.1
  • 33
    • 2942722444 scopus 로고    scopus 로고
    • Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers
    • Shorter, J., and S. Lindquist. 2004. Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science 304:1793-1797.
    • (2004) Science , vol.304 , pp. 1793-1797
    • Shorter, J.1    Lindquist, S.2
  • 34
    • 77949908054 scopus 로고    scopus 로고
    • AAA+ chaperone ClpX regulates dynamics of prokaryotic cytoskeletal protein FtsZ
    • Sugimoto, S., et al. 2010. AAA+ chaperone ClpX regulates dynamics of prokaryotic cytoskeletal protein FtsZ. J. Biol. Chem. 285:6648-6657.
    • (2010) J. Biol. Chem. , vol.285 , pp. 6648-6657
    • Sugimoto, S.1
  • 35
    • 78650910561 scopus 로고    scopus 로고
    • Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check
    • Tonthat, N. K., et al. 2011. Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check. EMBO J. 30:154-164.
    • (2011) EMBO J , vol.30 , pp. 154-164
    • Tonthat, N.K.1
  • 36
    • 0025941965 scopus 로고
    • A factor that positively regulates cell division by activating transcription of the major cluster of essential cell division genes of Escherichia coli
    • Wang, X. D., P. A. de Boer, and L. I. Rothfield. 1991. A factor that positively regulates cell division by activating transcription of the major cluster of essential cell division genes of Escherichia coli. EMBO J. 10:3363-3372.
    • (1991) EMBO J , vol.10 , pp. 3363-3372
    • Wang, X.D.1    de Boer, P.A.2    Rothfield, L.I.3
  • 37
    • 0037407703 scopus 로고    scopus 로고
    • Growth rate-dependent regulation of medial FtsZ ring formation
    • Weart, R. B., and P. A. Levin. 2003. Growth rate-dependent regulation of medial FtsZ ring formation. J. Bacteriol. 185:2826-2834.
    • (2003) J. Bacteriol. , vol.185 , pp. 2826-2834
    • Weart, R.B.1    Levin, P.A.2
  • 38
    • 21244497829 scopus 로고    scopus 로고
    • The ClpX chaperone modulates assembly of the tubulin-like protein FtsZ
    • Weart, R. B., S. Nakano, B. E. Lane, P. Zuber, and P. A. Levin. 2005. The ClpX chaperone modulates assembly of the tubulin-like protein FtsZ. Mol. Microbiol. 57:238-249.
    • (2005) Mol. Microbiol. , vol.57 , pp. 238-249
    • Weart, R.B.1    Nakano, S.2    Lane, B.E.3    Zuber, P.4    Levin, P.A.5
  • 39
    • 0033759546 scopus 로고    scopus 로고
    • Deletion of the min operon results in increased thermosensitivity of an ftsZ84 mutant and abnormal FtsZ ring assembly, placement, and disassembly
    • Yu, X. C., and W. Margolin. 2000. Deletion of the min operon results in increased thermosensitivity of an ftsZ84 mutant and abnormal FtsZ ring assembly, placement, and disassembly. J. Bacteriol. 182:6203-6213.
    • (2000) J. Bacteriol. , vol.182 , pp. 6203-6213
    • Yu, X.C.1    Margolin, W.2
  • 40
    • 0032895234 scopus 로고    scopus 로고
    • FtsZ ring clusters in min and partition mutants: role of both the Min system and the nucleoid in regulating FtsZ ring localization
    • Yu, X. C., and W. Margolin. 1999. FtsZ ring clusters in min and partition mutants: role of both the Min system and the nucleoid in regulating FtsZ ring localization. Mol. Microbiol. 32:315-326.
    • (1999) Mol. Microbiol. , vol.32 , pp. 315-326
    • Yu, X.C.1    Margolin, W.2


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