메뉴 건너뛰기




Volumn 216, Issue 1, 2002, Pages 23-32

Topological characterization of the essential Escherichia coli cell division protein FtsW

Author keywords

Cell division; FtsW; Lipid II; Topology

Indexed keywords

ALKALINE PHOSPHATASE; BACTERIAL PROTEIN; BETA LACTAMASE; PROTEIN BLA; PROTEIN FTSW; PROTEIN PHOA; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; FTSW PROTEIN, BACTERIA; MEMBRANE PROTEIN;

EID: 0037195381     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(02)00892-3     Document Type: Article
Times cited : (30)

References (25)
  • 2
    • 0025371804 scopus 로고
    • Nucleotide sequence involving murD and an open reading frame ORF-Y spacing murF and ftsW in Escherichia coli
    • Ikeda M., Wachi M., Ishino F., Matsuhashi M. Nucleotide sequence involving murD and an open reading frame ORF-Y spacing murF and ftsW in Escherichia coli. Nucleic Acids Res. 18:1990;1058.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 1058
    • Ikeda, M.1    Wachi, M.2    Ishino, F.3    Matsuhashi, M.4
  • 3
    • 0024439301 scopus 로고
    • Structural similarity among Escherichia coli FtsW and RodA proteins and Bacillus subtilis SpoVE protein, which function in cell division, cell elongation, and spore formation, respectively
    • Ikeda M., Sato T., Wachi M., Jung H.K., Ishino F., Kobayashi Y., Matsuhashi M. Structural similarity among Escherichia coli FtsW and RodA proteins and Bacillus subtilis SpoVE protein, which function in cell division, cell elongation, and spore formation, respectively. J. Bacteriol. 171:1989;6375-6378.
    • (1989) J. Bacteriol. , vol.171 , pp. 6375-6378
    • Ikeda, M.1    Sato, T.2    Wachi, M.3    Jung, H.K.4    Ishino, F.5    Kobayashi, Y.6    Matsuhashi, M.7
  • 4
    • 0025346860 scopus 로고
    • The life-cycle proteins RodA of E. coli and SpoVE of Bacillus subtilis have very similar primary structures
    • Joris B., Dive G., Henriques A., Piggot P.J., Ghuysen J.M. The life-cycle proteins RodA of E. coli and SpoVE of Bacillus subtilis have very similar primary structures. Mol. Microbiol. 4:(3):1990;513-517.
    • (1990) Mol. Microbiol. , vol.4 , Issue.3 , pp. 513-517
    • Joris, B.1    Dive, G.2    Henriques, A.3    Piggot, P.J.4    Ghuysen, J.M.5
  • 5
    • 10044253923 scopus 로고
    • Utilization of lipid-linked precursors and the formation of peptidoglycan in the process of cell growth and division: Membrane enzymes involved in the final steps of peptidoglycan synthesis and mechanism of their regulation
    • Ghuysen, J.-M. and Hakenbeck, R., Eds. Elsevier, Amsterdam
    • Matsuhashi, M. (1994) Utilization of lipid-linked precursors and the formation of peptidoglycan in the process of cell growth and division: Membrane enzymes involved in the final steps of peptidoglycan synthesis and mechanism of their regulation. In: Bacterial Cell Wall (Ghuysen, J.-M. and Hakenbeck, R., Eds.), pp. 55-71. Elsevier, Amsterdam.
    • (1994) Bacterial Cell Wall , pp. 55-71
    • Matsuhashi, M.1
  • 6
    • 85023011634 scopus 로고
    • Enzyme system involved in cell division in Escherichia coli: Septum peptidoglycan synthethase complex
    • Matsuhashi M., Pankrushina A.N., Ikeda M. Enzyme system involved in cell division in Escherichia coli: Septum peptidoglycan synthethase complex. J. Univ. Sci. Dev. Tokyo (Jpn.). 1:1991;183-200.
    • (1991) J. Univ. Sci. Dev. Tokyo (Jpn.) , vol.1 , pp. 183-200
    • Matsuhashi, M.1    Pankrushina, A.N.2    Ikeda, M.3
  • 7
    • 0030921172 scopus 로고    scopus 로고
    • The bimodular G57-V577 polypeptide chain of the class B penicillin-binding protein 3 of Escherichia coli catalyzes peptide bond formation from thiolesters and does not catalyze glycan chain polymerization from the lipid II intermediate
    • Adam M., Fraipont C., Rhazi N., Nguyen-Disteche M., Lakaye B., Frere J.M., Devreese B., Van Beeumen J., Van Heijenoort Y., Van Heijenoort J., Ghuysen J.M. The bimodular G57-V577 polypeptide chain of the class B penicillin-binding protein 3 of Escherichia coli catalyzes peptide bond formation from thiolesters and does not catalyze glycan chain polymerization from the lipid II intermediate. J. Bacteriol. 179:1997;6005-6009.
    • (1997) J. Bacteriol. , vol.179 , pp. 6005-6009
    • Adam, M.1    Fraipont, C.2    Rhazi, N.3    Nguyen-Disteche, M.4    Lakaye, B.5    Frere, J.M.6    Devreese, B.7    Van Beeumen, J.8    Van Heijenoort, Y.9    Van Heijenoort, J.10    Ghuysen, J.M.11
  • 8
    • 0028034240 scopus 로고
    • Identification of FtsW and characterization of a new ftsW division mutant of Escherichia coli
    • Khattar M.M., Begg K.J., Donachie W.D. Identification of FtsW and characterization of a new ftsW division mutant of Escherichia coli. J. Bacteriol. 176:1994;7140-7147.
    • (1994) J. Bacteriol. , vol.176 , pp. 7140-7147
    • Khattar, M.M.1    Begg, K.J.2    Donachie, W.D.3
  • 9
    • 0031016478 scopus 로고    scopus 로고
    • Two polypeptide products of the Escherichia coli cell division gene ftsW and a possible role for FtsW in FtsZ function
    • Khattar M.M., Addinall S.G., Stedul K.H., Boyle D.S., Lutkenhaus J., Donachie W.D. Two polypeptide products of the Escherichia coli cell division gene ftsW and a possible role for FtsW in FtsZ function. J. Bacteriol. 179:1997;784-793.
    • (1997) J. Bacteriol. , vol.179 , pp. 784-793
    • Khattar, M.M.1    Addinall, S.G.2    Stedul, K.H.3    Boyle, D.S.4    Lutkenhaus, J.5    Donachie, W.D.6
  • 11
    • 0032453738 scopus 로고    scopus 로고
    • FtsI and FtsW are localized to the septum in Escherichia coli
    • Wang L., Khattar M.K., Donachie W.D., Lutkenhaus J. FtsI and FtsW are localized to the septum in Escherichia coli. J. Bacteriol. 180:1998;2810-2816.
    • (1998) J. Bacteriol. , vol.180 , pp. 2810-2816
    • Wang, L.1    Khattar, M.K.2    Donachie, W.D.3    Lutkenhaus, J.4
  • 12
    • 0036155122 scopus 로고    scopus 로고
    • The Escherichia coli cell division protein FtsW is required to recruit its cognate transpeptidase, FtsI (PBP3), to the division site
    • Mercer K.L.N., Weiss D.S. The Escherichia coli cell division protein FtsW is required to recruit its cognate transpeptidase, FtsI (PBP3), to the division site. J. Bacteriol. 184:2002;904-912.
    • (2002) J. Bacteriol. , vol.184 , pp. 904-912
    • Mercer, K.L.N.1    Weiss, D.S.2
  • 13
    • 0036211844 scopus 로고    scopus 로고
    • Membrane topology of the Streptococcus pneumoniae FtsW division protein
    • Gerard P., Vernet T., Zapun A. Membrane topology of the Streptococcus pneumoniae FtsW division protein. J. Bacteriol. 184:2002;1925-1931.
    • (2002) J. Bacteriol. , vol.184 , pp. 1925-1931
    • Gerard, P.1    Vernet, T.2    Zapun, A.3
  • 15
    • 0000632797 scopus 로고
    • TnphoA: A transposon probe for protein export signals
    • Manoil C., Beckwith J. TnphoA: a transposon probe for protein export signals. Proc. Natl. Acad. Sci. USA. 82:1985;8129-8133.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 8129-8133
    • Manoil, C.1    Beckwith, J.2
  • 16
    • 0026052185 scopus 로고
    • Membrane topology analysis of Escherichia coli mannitol permease by using a nested-deletion method to create mtlA-phoA fusions
    • Sugiyama J.E., Mahmoodian S., Jacobson G.R. Membrane topology analysis of Escherichia coli mannitol permease by using a nested-deletion method to create mtlA-phoA fusions. Proc. Natl. Acad. Sci. USA. 88:1991;9603-9607.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9603-9607
    • Sugiyama, J.E.1    Mahmoodian, S.2    Jacobson, G.R.3
  • 17
    • 0032746748 scopus 로고    scopus 로고
    • Topological analysis of the MraY protein catalysing the first membrane step of peptidoglycan synthesis
    • Bouhss A., Mengin-Lecreulx D., Le Beller D., Van Heijenoort J. Topological analysis of the MraY protein catalysing the first membrane step of peptidoglycan synthesis. Mol. Microbiol. 34:1999;576-585.
    • (1999) Mol. Microbiol. , vol.34 , pp. 576-585
    • Bouhss, A.1    Mengin-Lecreulx, D.2    Le Beller, D.3    Van Heijenoort, J.4
  • 18
    • 0024416945 scopus 로고
    • Organization of the murE-murG region of Escherichia coli: Identification of the murD gene coding for the D-glutamic acid adding enzyme
    • Mengin-Lecreulx D., Parquet C., Desviat L.R., Plá J., Fluoret B., Ayala J.A., van Heijenoort J. Organization of the murE-murG region of Escherichia coli: Identification of the murD gene coding for the D-glutamic acid adding enzyme. J. Bacteriol. 171:1989;6126-6134.
    • (1989) J. Bacteriol. , vol.171 , pp. 6126-6134
    • Mengin-Lecreulx, D.1    Parquet, C.2    Desviat, L.R.3    Plá, J.4    Fluoret, B.5    Ayala, J.A.6    Van Heijenoort, J.7
  • 20
    • 0016700103 scopus 로고
    • Analysis of the regulation of Escherichia coli alkaline phosphatase synthesis using deletions and phi80 transducing phages
    • Brickman E., Beckwith J. Analysis of the regulation of Escherichia coli alkaline phosphatase synthesis using deletions and phi80 transducing phages. J. Mol. Biol. 96:1975;307-316.
    • (1975) J. Mol. Biol. , vol.96 , pp. 307-316
    • Brickman, E.1    Beckwith, J.2
  • 21
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence Adv
    • Chou P.Y., Fasman G.D. Prediction of the secondary structure of proteins from their amino acid sequence Adv. Enzymol. Relat. Areas Mol. Biol. 47:1978;45-148.
    • (1978) Enzymol. Relat. Areas Mol. Biol. , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 22
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 23
    • 0023028051 scopus 로고
    • A genetic approach to analyzing membrane protein topology
    • Manoil C., Beckwith J. A genetic approach to analyzing membrane protein topology. Science. 233:1986;1403-1408.
    • (1986) Science , vol.233 , pp. 1403-1408
    • Manoil, C.1    Beckwith, J.2
  • 24
    • 0023676242 scopus 로고
    • Topogenic signals in integral membrane proteins
    • von Heijne G., Gavel Y. Topogenic signals in integral membrane proteins. Eur. J. Biochem. 174:1988;671-678.
    • (1988) Eur. J. Biochem. , vol.174 , pp. 671-678
    • Von Heijne, G.1    Gavel, Y.2
  • 25
    • 0025330038 scopus 로고
    • Lac permease of Escherichia coli: Topology and sequence elements promoting membrane insertion
    • Calamia J., Manoil C. lac permease of Escherichia coli: topology and sequence elements promoting membrane insertion. Proc. Natl. Acad. Sci. USA. 87:1990;4937-4941.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4937-4941
    • Calamia, J.1    Manoil, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.