메뉴 건너뛰기




Volumn 192, Issue 23, 2010, Pages 6116-6125

Evidence from artificial septal targeting and site-directed mutagenesis that residues in the extracytoplasmic β domain of DivIB mediate its interaction with the divisomal transpeptidase PBP 2B

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; HETERODIMER; PROTEIN DIVIB; PROTEIN PBP 2 B; UNCLASSIFIED DRUG;

EID: 78649375524     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00783-10     Document Type: Article
Times cited : (13)

References (42)
  • 1
    • 0026059127 scopus 로고
    • FtsZ ring structure associated with division in Escherichia coli
    • Bi, E., and J. Lutkenhaus. 1991. FtsZ ring structure associated with division in Escherichia coli. Nature 354:161-164. (Pubitemid 21896803)
    • (1991) Nature , vol.354 , Issue.6349 , pp. 161-164
    • Bi, E.1    Lutkenhaus, J.2
  • 2
    • 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 J. Beckwith. 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
  • 3
    • 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., M. Minev, and J. Beckwith. 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
  • 5
    • 33750458379 scopus 로고    scopus 로고
    • Multiple interactions between the transmembrane division proteins of Bacillus subtilis and the role of FtsL instability in divisome assembly
    • Daniel, R. A., M. F. Noirot-Gros, P. Noirot, and J. Errington. 2006. Multiple interactions between the transmembrane division proteins of Bacillus subtilis and the role of FtsL instability in divisome assembly. J. Bacteriol. 188:7396-7404.
    • (2006) J. Bacteriol. , vol.188 , pp. 7396-7404
    • Daniel, R.A.1    Noirot-Gros, M.F.2    Noirot, P.3    Errington, J.4
  • 6
    • 0035977042 scopus 로고    scopus 로고
    • Crystal structure of PBP2x from a highly penicillin-resistant Streptococcus pneumoniae clinical isolate: A mosaic framework containing 83 mutations
    • Dessen, A., N. Mouz, E. Gordon, J. Hopkins, and O. Dideberg. 2001. Crystal structure of PBP2x from a highly penicillin-resistant Streptococcus pneumoniae clinical isolate: a mosaic framework containing 83 mutations. J. Biol. Chem. 276:45106-45112.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45106-45112
    • Dessen, A.1    Mouz, N.2    Gordon, E.3    Hopkins, J.4    Dideberg, O.5
  • 7
    • 0346252349 scopus 로고    scopus 로고
    • Use of a two-hybrid assay to study the assembly of a complex multicomponent protein machinery: Bacterial septosome differentiation
    • Di Lallo, G., M. Fagioli, D. Barionovi, P. Ghelardini, and L. Paolozzi. 2003. Use of a two-hybrid assay to study the assembly of a complex multicomponent protein machinery: bacterial septosome differentiation. Microbiology 149:3353-3359. (Pubitemid 38016664)
    • (2003) Microbiology , vol.149 , Issue.12 , pp. 3353-3359
    • Di Lallo, G.1    Fagioli, M.2    Barionovi, D.3    Ghelardini, P.4    Paolozzi, L.5
  • 8
    • 33846299252 scopus 로고    scopus 로고
    • Three functional domains of the Escherichia coli FtsQ protein are involved in its interaction with the other division proteins
    • D'Ulisse, V., M. Fagioli, P. Ghelardini, and L. Paolozzi. 2007. Three functional domains of the Escherichia coli FtsQ protein are involved in its interaction with the other division proteins. Microbiology 153:124-138.
    • (2007) Microbiology , vol.153 , pp. 124-138
    • D'Ulisse, V.1    Fagioli, M.2    Ghelardini, P.3    Paolozzi, L.4
  • 11
    • 21844441637 scopus 로고    scopus 로고
    • Diverse paths to midcell: Assembly of the bacterial cell division machinery
    • Goehring, N. W., and J. Beckwith. 2005. Diverse paths to midcell: assembly of the bacterial cell division machinery. Curr. Biol. 15:R514-R526.
    • (2005) Curr. Biol. , vol.15
    • Goehring, N.W.1    Beckwith, J.2
  • 12
    • 33745195461 scopus 로고    scopus 로고
    • Premature targeting of cell division proteins to midcell reveals hierarchies of protein interactions involved in divisome assembly
    • Goehring, N. W., M. D. Gonzalez, and J. Beckwith. 2006. Premature targeting of cell division proteins to midcell reveals hierarchies of protein interactions involved in divisome assembly. Mol. Microbiol. 61:33-45.
    • (2006) Mol. Microbiol. , vol.61 , pp. 33-45
    • Goehring, N.W.1    Gonzalez, M.D.2    Beckwith, J.3
  • 13
    • 33846237649 scopus 로고    scopus 로고
    • Mutants, suppressors, and wrinkled colonies: Mutant alleles of the cell division gene ftsQ point to functional domains in FtsQ and a role for domain 1C of FtsA in divisome assembly
    • Goehring, N. W., I. Petrovska, D. Boyd, and J. Beckwith. 2007. Mutants, suppressors, and wrinkled colonies: mutant alleles of the cell division gene ftsQ point to functional domains in FtsQ and a role for domain 1C of FtsA in divisome assembly. J. Bacteriol. 189:633-645.
    • (2007) J. Bacteriol. , vol.189 , pp. 633-645
    • Goehring, N.W.1    Petrovska, I.2    Boyd, D.3    Beckwith, J.4
  • 14
    • 77952577603 scopus 로고    scopus 로고
    • Multiple interaction domains in FtsL, a protein component of the widely conserved bacterial FtsLBQ cell division complex
    • Gonzalez, M. D., E. A. Akbay, D. Boyd, and J. Beckwith. 2010. Multiple interaction domains in FtsL, a protein component of the widely conserved bacterial FtsLBQ cell division complex. J. Bacteriol. 192:2757-2768.
    • (2010) J. Bacteriol. , vol.192 , pp. 2757-2768
    • Gonzalez, M.D.1    Akbay, E.A.2    Boyd, D.3    Beckwith, J.4
  • 15
    • 65249155295 scopus 로고    scopus 로고
    • Divisome under construction: Distinct domains of the small membrane protein FtsB are necessary for interaction with multiple cell division proteins
    • Gonzalez, M. D., and J. Beckwith. 2009. Divisome under construction: distinct domains of the small membrane protein FtsB are necessary for interaction with multiple cell division proteins. J. Bacteriol. 191:2815-2825.
    • (2009) J. Bacteriol. , vol.191 , pp. 2815-2825
    • Gonzalez, M.D.1    Beckwith, J.2
  • 16
    • 78649338546 scopus 로고    scopus 로고
    • FtsQ interaction mutants: A way to identify new antibacterial targets
    • 10 May doi:10.1016/j.nbt.2010.05.002
    • Grenga, L., G. Guglielmi, S. Melino, P. Ghelardini, and L. Paolozzi. 10 May 2010. FtsQ interaction mutants: a way to identify new antibacterial targets. N. Biotechnol. doi:10.1016/j.nbt.2010.05.002.
    • (2010) N. Biotechnol.
    • Grenga, L.1    Guglielmi, G.2    Melino, S.3    Ghelardini, P.4    Paolozzi, L.5
  • 17
    • 0027413114 scopus 로고
    • Characterization of mutations in divIB of Bacillus subtilis and cellular localization of the DivIB protein
    • Harry, E. J., B. J. Stewart, and R. G. Wake. 1993. Characterization of mutations in divIB of Bacillus subtilis and cellular localization of the DivIB protein. Mol. Microbiol. 7:611-621.
    • (1993) Mol. Microbiol. , vol.7 , pp. 611-621
    • Harry, E.J.1    Stewart, B.J.2    Wake, R.G.3
  • 18
    • 15244361175 scopus 로고    scopus 로고
    • Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis
    • Karimova, G., N. Dautin, and D. Ladant. 2005. Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis. J. Bacteriol. 187:2233-2243.
    • (2005) J. Bacteriol. , vol.187 , pp. 2233-2243
    • Karimova, G.1    Dautin, N.2    Ladant, D.3
  • 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 R. Losick. 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
    • 0033521857 scopus 로고    scopus 로고
    • GFP vectors for controlled expression and dual labelling of protein fusions in Bacillus subtilis
    • Lewis, P. J., and A. L. Marston. 1999. GFP vectors for controlled expression and dual labelling of protein fusions in Bacillus subtilis. Gene 227:101-109.
    • (1999) Gene , vol.227 , pp. 101-109
    • Lewis, P.J.1    Marston, A.L.2
  • 22
    • 42149131579 scopus 로고    scopus 로고
    • Cell-division inhibitors: New insights for future antibiotics
    • Lock, R. L., and E. J. Harry. 2008. Cell-division inhibitors: new insights for future antibiotics. Nat. Rev. Drug Discov. 7:324-338.
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 324-338
    • Lock, R.L.1    Harry, E.J.2
  • 23
    • 51349090440 scopus 로고    scopus 로고
    • Division protein interaction web: Identification of a phylogenetically conserved common interactome between Streptococcus pneumoniae and Escherichia coli
    • Maggi, S., O. Massidda, G. Luzi, D. Fadda, L. Paolozzi, and P. Ghelardini. 2008. Division protein interaction web: identification of a phylogenetically conserved common interactome between Streptococcus pneumoniae and Escherichia coli. Microbiology 154:3042-3052.
    • (2008) Microbiology , vol.154 , pp. 3042-3052
    • Maggi, S.1    Massidda, O.2    Luzi, G.3    Fadda, D.4    Paolozzi, L.5    Ghelardini, P.6
  • 24
    • 27644540151 scopus 로고    scopus 로고
    • FtsZ and the division of prokarytotic cells and organelles
    • Margolin, W. 2005. FtsZ and the division of prokarytotic cells and organelles. Nat. Rev. Mol. Cell Biol. 6:862-871.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 862-871
    • Margolin, W.1
  • 26
    • 0029988098 scopus 로고    scopus 로고
    • X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme
    • Pares, S., N. Mouz, Y. Petillot, R. Hakenbeck, and O. Dideberg. 1996. X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme. Nat. Struct. Biol. 3:284-289.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 284-289
    • Pares, S.1    Mouz, N.2    Petillot, Y.3    Hakenbeck, R.4    Dideberg, O.5
  • 27
    • 1942437430 scopus 로고    scopus 로고
    • A PBP2x from a clinical isolate of Streptococcus pneumoniae exhibits an alternative mechanism for reduction of susceptibility to β-lactam antibiotics
    • Pernot, L., L. Chesnel, A. Le Gouellec, J. Croize, T. Vernet, O. Dideberg, and A. Dessen. 2004. A PBP2x from a clinical isolate of Streptococcus pneumoniae exhibits an alternative mechanism for reduction of susceptibility to β-lactam antibiotics. J. Biol. Chem. 279:16463-16470.
    • (2004) J. Biol. Chem. , vol.279 , pp. 16463-16470
    • Pernot, L.1    Chesnel, L.2    Le Gouellec, A.3    Croize, J.4    Vernet, T.5    Dideberg, O.6    Dessen, A.7
  • 28
    • 4444297890 scopus 로고    scopus 로고
    • Structural determinants required to target penicillin-binding protein 3 to the septum of Escherichia coli
    • Piette, A., C. Fraipont, T. Den Blaauwen, M. E. Aarsman, S. Pastoret, and M. Nguyen-Disteche. 2004. Structural determinants required to target penicillin-binding protein 3 to the septum of Escherichia coli. J. Bacteriol. 186: 6110-6117.
    • (2004) J. Bacteriol. , vol.186 , pp. 6110-6117
    • Piette, A.1    Fraipont, C.2    Den Blaauwen, T.3    Aarsman, M.E.4    Pastoret, S.5    Nguyen-Disteche, M.6
  • 29
    • 33644770635 scopus 로고    scopus 로고
    • Localization of the Bacillus subtilis murB gene within the dcw cluster is important for growth and sporulation
    • Real, G., and A. O. Henriques. 2006. Localization of the Bacillus subtilis murB gene within the dcw cluster is important for growth and sporulation. J. Bacteriol. 188:1721-1732.
    • (2006) J. Bacteriol. , vol.188 , pp. 1721-1732
    • Real, G.1    Henriques, A.O.2
  • 30
    • 51549084792 scopus 로고    scopus 로고
    • Artificial septal targeting of Bacillus subtilis cell division proteins in Escherichia coli: An interspecies approach to the study of protein-protein interactions in multiprotein complexes
    • Robichon, C., G. F. King, N. W. Goehring, and J. Beckwith. 2008. Artificial septal targeting of Bacillus subtilis cell division proteins in Escherichia coli: an interspecies approach to the study of protein-protein interactions in multiprotein complexes. J. Bacteriol. 190:6048-6059.
    • (2008) J. Bacteriol. , vol.190 , pp. 6048-6059
    • Robichon, C.1    King, G.F.2    Goehring, N.W.3    Beckwith, J.4
  • 31
    • 33646269969 scopus 로고    scopus 로고
    • Domain architecture and structure of the bacterial cell division protein DivIB
    • Robson, S. A., and G. F. King. 2006. Domain architecture and structure of the bacterial cell division protein DivIB. Proc. Natl. Acad. Sci. U. S. A. 103:6700-6705.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 6700-6705
    • Robson, S.A.1    King, G.F.2
  • 32
    • 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., K. A. Michie, J. P. Mackay, E. Harry, and G. F. King. 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
  • 33
    • 0242693139 scopus 로고    scopus 로고
    • Assembly dynamics of the bacterial cell division protein FtsZ: Poised at the edge of stability
    • Romberg, L., and P. A. Levin. 2003. Assembly dynamics of the bacterial cell division protein FtsZ: poised at the edge of stability. Annu. Rev. Microbiol. 57:125-154.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 125-154
    • Romberg, L.1    Levin, P.A.2
  • 34
    • 0034029042 scopus 로고    scopus 로고
    • The Bacillus subtilis cell division protein FtsL localizes to sites of septation and interacts with DivIC
    • Sievers, J., and J. Errington. 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
  • 35
    • 33750432185 scopus 로고    scopus 로고
    • Requirement for the cell division protein DivIB in polar cell division and engulfment during sporulation in Bacillus subtilis
    • Thompson, L. S., P. L. Beech, G. Real, A. O. Henriques, and E. J. Harry. 2006. Requirement for the cell division protein DivIB in polar cell division and engulfment during sporulation in Bacillus subtilis. J. Bacteriol. 188:7677-7685.
    • (2006) J. Bacteriol. , vol.188 , pp. 7677-7685
    • Thompson, L.S.1    Beech, P.L.2    Real, G.3    Henriques, A.O.4    Harry, E.J.5
  • 38
    • 38849174785 scopus 로고    scopus 로고
    • The divisomal protein DivIB contains multiple epitopes that mediate its recruitment to incipient division sites
    • Wadsworth, K. D., S. L. Rowland, E. J. Harry, and G. F. King. 2008. The divisomal protein DivIB contains multiple epitopes that mediate its recruitment to incipient division sites. Mol. Microbiol. 67:1143-1155.
    • (2008) Mol. Microbiol. , vol.67 , pp. 1143-1155
    • Wadsworth, K.D.1    Rowland, S.L.2    Harry, E.J.3    King, G.F.4
  • 39
    • 7644219685 scopus 로고    scopus 로고
    • Bacterial cell division and the septal ring
    • Weiss, D. S. 2004. Bacterial cell division and the septal ring. Mol. Microbiol. 54:588-597.
    • (2004) Mol. Microbiol. , vol.54 , pp. 588-597
    • Weiss, D.S.1
  • 40
    • 0032932435 scopus 로고    scopus 로고
    • Localization of FtsI (PBP3) to the septal ring requires its membrane anchor, the Z ring, FtsA, FtsQ, and FtsL
    • Weiss, D. S., J. C. Chen, J.-M. Ghigo, D. Boyd, and J. Beckwith. 1999. Localization of FtsI (PBP3) to the septal ring requires its membrane anchor, the Z ring, FtsA, FtsQ, and FtsL. J. Bacteriol. 181:508-520.
    • (1999) J. Bacteriol. , vol.181 , pp. 508-520
    • Weiss, D.S.1    Chen, J.C.2    Ghigo, J.-M.3    Boyd, D.4    Beckwith, J.5
  • 41
    • 0347915664 scopus 로고    scopus 로고
    • Genetic analysis of the cell division protein FtsI (PBP3): Amino acid substitutions that impair septal localization of FtsI and recruitment of FtsN
    • Wissel, M. C., and D. S. Weiss. 2004. Genetic analysis of the cell division protein FtsI (PBP3): amino acid substitutions that impair septal localization of FtsI and recruitment of FtsN. J. Bacteriol. 186:490-502.
    • (2004) J. Bacteriol. , vol.186 , pp. 490-502
    • Wissel, M.C.1    Weiss, D.S.2
  • 42
    • 11144318755 scopus 로고    scopus 로고
    • The transmembrane helix of the Escherichia coli division protein FtsI localizes to the septal ring
    • Wissel, M. C., J. L. Wendt, C. J. Mitchell, and D. S. Weiss. 2005. The transmembrane helix of the Escherichia coli division protein FtsI localizes to the septal ring. J. Bacteriol. 187:320-328.
    • (2005) J. Bacteriol. , vol.187 , pp. 320-328
    • Wissel, M.C.1    Wendt, J.L.2    Mitchell, C.J.3    Weiss, D.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.