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Volumn 55, Issue 2, 2005, Pages 413-424

In vitro reconstitution of a trimeric complex of DivIB, DivIC and FtsL, and their transient co-localization at the division site in Streptococcus pneumoniae

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PROTEIN DIVIB; PROTEIN DIVIC; PROTEIN FTSL; UNCLASSIFIED DRUG;

EID: 13144257721     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2004.04408.x     Document Type: Article
Times cited : (62)

References (26)
  • 1
    • 0037169328 scopus 로고    scopus 로고
    • FtsK is a DNA motor protein that activates chromosome dimer resolution by switching the catalytic state of the XerC and XerD recombinases
    • Aussel, L., Barre, F.X., Aroyo, M., Stasiak, A., Stasiak, A.Z., and Sherratt, D. (2002) FtsK is a DNA motor protein that activates chromosome dimer resolution by switching the catalytic state of the XerC and XerD recombinases. Cell 108: 195-205.
    • (2002) Cell , vol.108 , pp. 195-205
    • Aussel, L.1    Barre, F.X.2    Aroyo, M.3    Stasiak, A.4    Stasiak, A.Z.5    Sherratt, D.6
  • 2
    • 0036900016 scopus 로고    scopus 로고
    • Assembly of cell division proteins at the E. coli cell center
    • Buddelmeijer, N., and Beckwith, J. (2002) Assembly of cell division proteins at the E. coli cell center. Curr Opin Microbiol 5: 553-557.
    • (2002) Curr Opin Microbiol , vol.5 , pp. 553-557
    • Buddelmeijer, N.1    Beckwith, J.2
  • 3
    • 2942570076 scopus 로고    scopus 로고
    • A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region
    • Buddelmeijer, N., and Beckwith, J. (2004) A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region. Mol Microbiol 52: 1315-1327.
    • (2004) Mol Microbiol , vol.52 , pp. 1315-1327
    • Buddelmeijer, N.1    Beckwith, J.2
  • 4
    • 0037197976 scopus 로고    scopus 로고
    • YgbQ, a cell division protein in Escherichia coli and Vibrio cholerae, localizes in codependent fashion with FtsL to the division site
    • Buddelmeijer, N., Judson, N., Boyd, D., Mekalanos, J.J., and Beckwith, J. (2002) YgbQ, a cell division protein in Escherichia coli and Vibrio cholerae, localizes in codependent fashion with FtsL to the division site. Proc Natl Acad Sci USA 99: 6316-6321.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6316-6321
    • Buddelmeijer, N.1    Judson, N.2    Boyd, D.3    Mekalanos, J.J.4    Beckwith, J.5
  • 5
    • 0029812117 scopus 로고    scopus 로고
    • Kinetic study on the formation of a de novo designed heterodimeric coiled-coil: Use of surface plasmon resonance to monitor the association and dissociation of polypeptide chains
    • Chao, H., Houston, M.E., Jr, Grothe, S., Kay, C.M., O'Connor-McCourt, M., Irvin, R.T., and Hodges, R.S. (1996) Kinetic study on the formation of a de novo designed heterodimeric coiled-coil: use of surface plasmon resonance to monitor the association and dissociation of polypeptide chains. Biochemistry 35: 12175-12185.
    • (1996) Biochemistry , vol.35 , pp. 12175-12185
    • Chao, H.1    Houston Jr., M.E.2    Grothe, S.3    Kay, C.M.4    O'Connor-McCourt, M.5    Irvin, R.T.6    Hodges, R.S.7
  • 6
    • 0032953197 scopus 로고    scopus 로고
    • Septal localization of FtsQ, an essential cell division protein in Escherichia coli
    • Chen, J.C., Weiss, D.S., Ghigo, J.M., and Beckwith, J. (1999) Septal localization of FtsQ, an essential cell division protein in Escherichia coli. J Bacteriol 181: 521-530.
    • (1999) J Bacteriol , vol.181 , pp. 521-530
    • Chen, J.C.1    Weiss, D.S.2    Ghigo, J.M.3    Beckwith, J.4
  • 7
    • 0036176969 scopus 로고    scopus 로고
    • Analysis of ftsQ mutant alleles in Escherichia coli: Complementation, septal localization, and recruitment of downstream cell division proteins
    • Chen, J.C., Minev, M., and Beckwith, J. (2002) Analysis of ftsQ mutant alleles in Escherichia coli: complementation, septal localization, and recruitment of downstream cell division proteins. J Bacteriol 184: 695-705.
    • (2002) J Bacteriol , vol.184 , pp. 695-705
    • Chen, J.C.1    Minev, M.2    Beckwith, J.3
  • 8
    • 0034107581 scopus 로고    scopus 로고
    • Intrinsic instability of the essential cell division protein FtsL of Bacillus subtilis and a role for DivIB protein in FtsL turnover
    • Daniel, R.A., and Errington, J. (2000) Intrinsic instability of the essential cell division protein FtsL of Bacillus subtilis and a role for DivIB protein in FtsL turnover. Mol Microbiol 36: 278-289.
    • (2000) Mol Microbiol , vol.36 , pp. 278-289
    • Daniel, R.A.1    Errington, J.2
  • 9
    • 0031824694 scopus 로고    scopus 로고
    • Characterization of the essential cell division gene ftsL(yIID) of Bacillus subtilis and its role in the assembly of the division apparatus
    • Daniel, R.A., Harry, E.J., Katis, V.L., Wake, R.G., and Errington, J. (1998) Characterization of the essential cell division gene ftsL(yIID) of Bacillus subtilis and its role in the assembly of the division apparatus. Mol Microbiol 29: 593-604.
    • (1998) Mol Microbiol , vol.29 , pp. 593-604
    • Daniel, R.A.1    Harry, E.J.2    Katis, V.L.3    Wake, R.G.4    Errington, J.5
  • 10
    • 78651153791 scopus 로고
    • Disc electrophoresis. Ii. Method and application to human serum proteins
    • Davis, B.J. (1964) Disc electrophoresis. Ii. Method and application to human serum proteins. Ann N Y Acad Sci 121: 404-427.
    • (1964) Ann N Y Acad Sci , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 11
    • 0031720923 scopus 로고    scopus 로고
    • Only the N-terminal domain of FtsK functions in cell division
    • Draper, G.C., McLennan, N., Begg, K., Masters, M., and Donachie, W.D. (1998) Only the N-terminal domain of FtsK functions in cell division. J Bacteriol 180: 4621-4627.
    • (1998) J Bacteriol , vol.180 , pp. 4621-4627
    • Draper, G.C.1    McLennan, N.2    Begg, K.3    Masters, M.4    Donachie, W.D.5
  • 13
    • 0033986953 scopus 로고    scopus 로고
    • Cell division in Escherichia coli: Role of FtsL domains in septal localization, function, and oligomerization
    • Ghigo, J.M., and Beckwith, J. (2000) Cell division in Escherichia coli: role of FtsL domains in septal localization, function, and oligomerization. J Bacteriol 182: 116-129.
    • (2000) J Bacteriol , vol.182 , pp. 116-129
    • Ghigo, J.M.1    Beckwith, J.2
  • 15
    • 0027062784 scopus 로고
    • FtsL, an essential cytoplasmic membrane protein involved in cell division in Escherichia coli
    • Guzman, L.M., Barondess, J.J., and Beckwith, J. (1992) FtsL, an essential cytoplasmic membrane protein involved in cell division in Escherichia coli. J Bacteriol 174: 7716-7728.
    • (1992) J Bacteriol , vol.174 , pp. 7716-7728
    • Guzman, L.M.1    Barondess, J.J.2    Beckwith, J.3
  • 16
    • 0030756250 scopus 로고    scopus 로고
    • Domain-swapping analysis of FtsI, FtsL, and FtsQ, bitopic membrane proteins essential for cell division in Escherichia coli
    • Guzman, L.M., Weiss, D.S., and Beckwith, J. (1997) Domain-swapping analysis of FtsI, FtsL, and FtsQ, bitopic membrane proteins essential for cell division in Escherichia coli. J Bacteriol 179: 5094-5103.
    • (1997) J Bacteriol , vol.179 , pp. 5094-5103
    • Guzman, L.M.1    Weiss, D.S.2    Beckwith, J.3
  • 17
    • 0032953633 scopus 로고    scopus 로고
    • Membrane-bound division proteins DivIB and DivIC of Bacillus subtilis function solely through their external domains in both vegetative and sporulation division
    • Katis, V.L., and Wake, R.G. (1999) Membrane-bound division proteins DivIB and DivIC of Bacillus subtilis function solely through their external domains in both vegetative and sporulation division. J Bacteriol 181: 2710-2718.
    • (1999) J Bacteriol , vol.181 , pp. 2710-2718
    • Katis, V.L.1    Wake, R.G.2
  • 18
    • 0034114854 scopus 로고    scopus 로고
    • Septal localization of the membrane-bound division proteins of Bacillus subtilis DivIB and DivIC is codependent only at high temperatures and requires FtsZ
    • Katis, V.L., Wake, R.G., and Harry, E.J. (2000) Septal localization of the membrane-bound division proteins of Bacillus subtilis DivIB and DivIC is codependent only at high temperatures and requires FtsZ. J Bacteriol 182: 3607-3611.
    • (2000) J Bacteriol , vol.182 , pp. 3607-3611
    • Katis, V.L.1    Wake, R.G.2    Harry, E.J.3
  • 19
    • 0025129872 scopus 로고
    • Hydrophobic cluster analysis: Procedures to derive structural and functional information from 2-D-representation of protein sequences
    • Lemesle-Varloot, L., Henrissat, B., Gaboriaud, C., Bissery, V., Morgat, A., and Mornon, J.P. (1990) Hydrophobic cluster analysis: procedures to derive structural and functional information from 2-D-representation of protein sequences. Biochimie 72: 555-574.
    • (1990) Biochimie , vol.72 , pp. 555-574
    • Lemesle-Varloot, L.1    Henrissat, B.2    Gaboriaud, C.3    Bissery, V.4    Morgat, A.5    Mornon, J.P.6
  • 20
    • 0028294868 scopus 로고
    • Characterization of a cell division gene from Bacillus subtilis that is required for vegetative and sporulation septum formation
    • Levin, P.A., and Losick, R. (1994) Characterization of a cell division gene from Bacillus subtilis that is required for vegetative and sporulation septum formation. J Bacteriol 176: 1451-1459.
    • (1994) J Bacteriol , vol.176 , pp. 1451-1459
    • Levin, P.A.1    Losick, R.2
  • 21
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • Lupas, A. (1996) Coiled coils: new structures and new functions. Trends Biochem Sci 21: 375-382.
    • (1996) Trends Biochem Sci , vol.21 , pp. 375-382
    • Lupas, A.1
  • 22
    • 1642442760 scopus 로고    scopus 로고
    • The D,D,-carboxypeptidase PBP3 organizes the division process of Streptococcus pneumoniae
    • Morlot, C., Noirclerc-Savoye, M., Zapun, A., Dideberg, O., and Vernet, T. (2004) The D,D,-carboxypeptidase PBP3 organizes the division process of Streptococcus pneumoniae. Mol Microbiol 51: 1641-1648.
    • (2004) Mol Microbiol , vol.51 , pp. 1641-1648
    • Morlot, C.1    Noirclerc-Savoye, M.2    Zapun, A.3    Dideberg, O.4    Vernet, T.5
  • 23
    • 0242437870 scopus 로고    scopus 로고
    • Growth and division of Streptococcus pneumoniae: Localization of the high molecular weight penicillin-binding proteins during the cell cycle
    • Morlot, C., Zapun, A., Dideberg, O., and Vernet, T. (2003) Growth and division of Streptococcus pneumoniae: localization of the high molecular weight penicillin-binding proteins during the cell cycle. Mol Microbiol 50: 845-855.
    • (2003) Mol Microbiol , vol.50 , pp. 845-855
    • Morlot, C.1    Zapun, A.2    Dideberg, O.3    Vernet, T.4
  • 24
    • 0022489523 scopus 로고
    • Activity of penicillin-binding protein 3 from Escherichia coli
    • Pisabarro, A.G., Prats, R., Vaquez, D., and Rodriguez-Tebar, A. (1986) Activity of penicillin-binding protein 3 from Escherichia coli. J Bacteriol 168: 199-206.
    • (1986) J Bacteriol , vol.168 , pp. 199-206
    • Pisabarro, A.G.1    Prats, R.2    Vaquez, D.3    Rodriguez-Tebar, A.4
  • 25
    • 0036096858 scopus 로고    scopus 로고
    • The Bacillus subtilis cell division proteins FtsL and DivIC are intrinsically unstable and do not interact with one another in the absence of other septasomal components
    • Robson, S.A., Michie, K.A., Mackay, J.P., Harry, E., and King, G.F. (2002) The Bacillus subtilis cell division proteins FtsL and DivIC are intrinsically unstable and do not interact with one another in the absence of other septasomal components. Mol Microbiol 44: 663-674.
    • (2002) Mol Microbiol , vol.44 , pp. 663-674
    • Robson, S.A.1    Michie, K.A.2    Mackay, J.P.3    Harry, E.4    King, G.F.5
  • 26
    • 0034029042 scopus 로고    scopus 로고
    • The Bacillus subtilis cell division protein FtsL localizes to sites of septation and interacts with DivIC
    • Sievers, J., and Errington, J. (2000) The Bacillus subtilis cell division protein FtsL localizes to sites of septation and interacts with DivIC. Mol Microbiol 36: 846-855.
    • (2000) Mol Microbiol , vol.36 , pp. 846-855
    • Sievers, J.1    Errington, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.