메뉴 건너뛰기




Volumn 179, Issue 16, 1997, Pages 5094-5103

Domain-swapping analysis of FtsI, FtsL, and FtsQ, bitopic membrane proteins essential for cell division in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; BACTERIAL GROWTH; CELL DIVISION; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN LOCALIZATION;

EID: 0030756250     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.16.5094-5103.1997     Document Type: Article
Times cited : (81)

References (47)
  • 2
    • 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.
    • (1991) Nature , vol.354 , pp. 161-164
    • Bi, E.1    Lutkenhaus, J.2
  • 3
    • 0025885341 scopus 로고
    • Role of potentially charged transmembrane residues in targeting proteins for retention and degradation within the endoplasmic reticulum
    • Bonifacino, J. S., P. Cosson, N. Shah, and R. D. Klausner. 1991. Role of potentially charged transmembrane residues in targeting proteins for retention and degradation within the endoplasmic reticulum. EMBO J. 10:2783-2793.
    • (1991) EMBO J. , vol.10 , pp. 2783-2793
    • Bonifacino, J.S.1    Cosson, P.2    Shah, N.3    Klausner, R.D.4
  • 4
    • 0024445203 scopus 로고
    • Membrane topology of penicillin-binding protein 3 of Escherichia coli
    • Bowler, L. D., and B. G. Spratt. 1989. Membrane topology of penicillin-binding protein 3 of Escherichia coli. Mol. Microbiol. 3:1277-1286.
    • (1989) Mol. Microbiol. , vol.3 , pp. 1277-1286
    • Bowler, L.D.1    Spratt, B.G.2
  • 5
    • 0024372724 scopus 로고
    • Positively charged amino acid residues can act as topogenic determinants in membrane proteins
    • Boyd, D., and J. Beckwith. 1989. Positively charged amino acid residues can act as topogenic determinants in membrane proteins. Proc. Natl. Acad. Sci. USA 86:9446-9450.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9446-9450
    • Boyd, D.1    Beckwith, J.2
  • 7
    • 0025803531 scopus 로고
    • The FtsQ protein of Escherichia coli: Membrane topology, abundance, and cell division phenotypes due to overproduction and insertion mutations
    • Carson, M. J., J. Barondess, and J. Beckwith. 1991. The FtsQ protein of Escherichia coli: membrane topology, abundance, and cell division phenotypes due to overproduction and insertion mutations. J. Bacteriol. 173:2187-2195.
    • (1991) J. Bacteriol. , vol.173 , pp. 2187-2195
    • Carson, M.J.1    Barondess, J.2    Beckwith, J.3
  • 8
    • 85036489803 scopus 로고    scopus 로고
    • Carson, M. J., and J. Beckwith. Unpublished data
    • Carson, M. J., and J. Beckwith. Unpublished data.
  • 9
    • 0025819126 scopus 로고
    • Membrane protein association by potential intramembrane charge pairs
    • Cosson, P., S. P. Lankford, J. S. Bonifacino, and R. D. Klausner. 1991. Membrane protein association by potential intramembrane charge pairs. Nature 351:414-416.
    • (1991) Nature , vol.351 , pp. 414-416
    • Cosson, P.1    Lankford, S.P.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 10
    • 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
  • 11
    • 0029863071 scopus 로고    scopus 로고
    • Topological characterization of the essential Escherichia coli cell division protein FtsN
    • Dai, K., V. F. Xu, and J. Lutkenhaus. 1996. Topological characterization of the essential Escherichia coli cell division protein FtsN. J. Bacteriol. 178: 1328-1334.
    • (1996) J. Bacteriol. , vol.178 , pp. 1328-1334
    • Dai, K.1    Xu, V.F.2    Lutkenhaus, J.3
  • 12
    • 0029956443 scopus 로고    scopus 로고
    • Direct quantitation of the number of individual penicillin-binding proteins per cell in Escherichia coli
    • Dougherty, T. J., K. Kennedy, R. E. Kessler, and M. J. Pucci. 1996. Direct quantitation of the number of individual penicillin-binding proteins per cell in Escherichia coli. J. Bacteriol. 178:6110-6115.
    • (1996) J. Bacteriol. , vol.178 , pp. 6110-6115
    • Dougherty, T.J.1    Kennedy, K.2    Kessler, R.E.3    Pucci, M.J.4
  • 13
    • 0025947624 scopus 로고
    • Proper insertion of a complex membrane protein in the absence of its amino-terminal export signal
    • Ehrmann, M., and J. Beckwith. 1991. Proper insertion of a complex membrane protein in the absence of its amino-terminal export signal. J. Biol. Chem. 266:16530-16533.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16530-16533
    • Ehrmann, M.1    Beckwith, J.2
  • 15
    • 0021161867 scopus 로고
    • The nucleotide sequence of the gene for malF protein, an inner membrane component of the maltose transport system of Escherichia coli
    • Froshauer, S., and J. Beckwith. 1984. The nucleotide sequence of the gene for malF protein, an inner membrane component of the maltose transport system of Escherichia coli. J. Biol. Chem. 259:10896-10903.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10896-10903
    • Froshauer, S.1    Beckwith, J.2
  • 16
    • 0028173341 scopus 로고
    • Molecular structures of penicillin-binding proteins and β-lactamases
    • Ghuysen, J. M. 1994. Molecular structures of penicillin-binding proteins and β-lactamases. Trends Microbiol. 2:372-380.
    • (1994) Trends Microbiol. , vol.2 , pp. 372-380
    • Ghuysen, J.M.1
  • 17
    • 0029808359 scopus 로고    scopus 로고
    • The non-penicillin-binding module of the tripartite penicillin-binding protein 3 of Escherichia coli is required for folding and/or stability of the penicillin-binding module and the membrane-anchoring module confers cell septation activity on the folded structure
    • Goffin, C., C. Fraipont, J. Ayala, M. Terrak, M. Nguyen-Distèche, and J.-M. Ghuysen. 1996. The non-penicillin-binding module of the tripartite penicillin-binding protein 3 of Escherichia coli is required for folding and/or stability of the penicillin-binding module and the membrane-anchoring module confers cell septation activity on the folded structure. J. Bacteriol. 178:5402-5409.
    • (1996) J. Bacteriol. , vol.178 , pp. 5402-5409
    • Goffin, C.1    Fraipont, C.2    Ayala, J.3    Terrak, M.4    Nguyen-Distèche, M.5    Ghuysen, J.-M.6
  • 18
    • 0027396163 scopus 로고
    • The motif Tyr-X-X-hydrophobic residue mediates lysosomal membrane targeting of lysosome-associated membrane protein 1
    • Guarnieri, F. G., L. M. Arterburn, M. B. Penno, Y. Cha, and J. T. August. 1993. The motif Tyr-X-X-hydrophobic residue mediates lysosomal membrane targeting of lysosome-associated membrane protein 1. J. Biol. Chem. 268:1941-1946.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1941-1946
    • Guarnieri, F.G.1    Arterburn, L.M.2    Penno, M.B.3    Cha, Y.4    August, J.T.5
  • 19
    • 85036492260 scopus 로고    scopus 로고
    • Guzman, L.-M. Unpublished results
    • Guzman, L.-M. Unpublished results.
  • 20
    • 0027062784 scopus 로고
    • FtsL, an essential cytoplasmic membrane protein involved in cell division in Escherichia coli
    • Guzman, L.-M., J. J. Barondess, and J. Beckwith. 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
  • 21
    • 85036480506 scopus 로고    scopus 로고
    • Guzman, L.-M., and J. Beckwith. Unpublished results
    • 18a. Guzman, L.-M., and J. Beckwith. Unpublished results.
  • 23
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson, R., J. M. Baldwin, T. A. Ceska, F. Zemlin, E. Beckmann, and K. H. Downing. 1990. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213:899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 24
    • 0015994375 scopus 로고
    • Divergent operons and the genetic structure of the maltose B region in Escherichia coli K-12
    • Hofnung, M. 1974. Divergent operons and the genetic structure of the maltose B region in Escherichia coli K-12. Genetics 76:169-184.
    • (1974) Genetics , vol.76 , pp. 169-184
    • Hofnung, M.1
  • 25
    • 0019819673 scopus 로고
    • Peptidoglycan synthetic enzyme activities of highly purified penicillin-binding protein 3 in E. coli: A septum-forming reaction sequence
    • Ishino, F., and M. Matsuhashi. 1981. Peptidoglycan synthetic enzyme activities of highly purified penicillin-binding protein 3 in E. coli: a septum-forming reaction sequence. Biochem. Biophys. Res. Commun. 101:905-911.
    • (1981) Biochem. Biophys. Res. Commun. , vol.101 , pp. 905-911
    • Ishino, F.1    Matsuhashi, M.2
  • 28
    • 0025899560 scopus 로고
    • Decoding signals for membrane protein assembly using alkaline phosphatase fusions
    • McGovern, K., M. Ehrmann, and J. Beckwith. 1991. Decoding signals for membrane protein assembly using alkaline phosphatase fusions. EMBO J. 10:2773-2782.
    • (1991) EMBO J. , vol.10 , pp. 2773-2782
    • McGovern, K.1    Ehrmann, M.2    Beckwith, J.3
  • 29
    • 0025100516 scopus 로고
    • Differential translation of cell division proteins
    • Mukherjee, A., and W. D. Donachie. 1990. Differential translation of cell division proteins. J. Bacteriol. 172:6106-6111.
    • (1990) J. Bacteriol. , vol.172 , pp. 6106-6111
    • Mukherjee, A.1    Donachie, W.D.2
  • 30
    • 0028334912 scopus 로고
    • Residues essential for the function of SecE, a membrane component of the Escherichia coli secretion apparatus, are located in a conserved cytoplasmic region
    • Murphy, C. K., and J. Beckwith. 1994. Residues essential for the function of SecE, a membrane component of the Escherichia coli secretion apparatus, are located in a conserved cytoplasmic region. Proc. Natl. Acad. Sci. USA 91:2557-2561.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2557-2561
    • Murphy, C.K.1    Beckwith, J.2
  • 31
    • 0024439293 scopus 로고
    • Determination of the cleavage site involved in C-terminal processing of penicillin-binding protein 3 of Escherichia coli
    • Nagasawa, H., Y. Sakagami, A. Suzuki, H. Suzuki, H. Hara, and Y. Hirota. 1989. Determination of the cleavage site involved in C-terminal processing of penicillin-binding protein 3 of Escherichia coli. J. Bacteriol. 171:5890-5893.
    • (1989) J. Bacteriol. , vol.171 , pp. 5890-5893
    • Nagasawa, H.1    Sakagami, Y.2    Suzuki, A.3    Suzuki, H.4    Hara, H.5    Hirota, Y.6
  • 32
    • 0025015646 scopus 로고
    • Fine-tuning the topology of a polytopic membrane protein. Role of positively and negatively charged amino acids
    • Nilsson, I., and G. von Heijne. 1990. Fine-tuning the topology of a polytopic membrane protein. Role of positively and negatively charged amino acids. Cell 62:1135-1141.
    • (1990) Cell , vol.62 , pp. 1135-1141
    • Nilsson, I.1    Von Heijne, G.2
  • 33
    • 0026072695 scopus 로고
    • The membrane spanning domain of β-1,4-galactosyltransferase specifies trans Golgi localization
    • Nilsson, T., J. M. Lucocq, D. Mackay, and G. Warren. 1991. The membrane spanning domain of β-1,4-galactosyltransferase specifies trans Golgi localization. EMBO J. 10:3567-3575.
    • (1991) EMBO J. , vol.10 , pp. 3567-3575
    • Nilsson, T.1    Lucocq, J.M.2    Mackay, D.3    Warren, G.4
  • 34
    • 0027204816 scopus 로고
    • Membrane protein retention in the yeast Golgi apparatus: Dipeptidyl aminopeptidase A is retained by a cytoplasmic signal containing aromatic residues
    • Nothwehr, S. F., C. J. Roberts, and T. H. Stevens. 1993. Membrane protein retention in the yeast Golgi apparatus: dipeptidyl aminopeptidase A is retained by a cytoplasmic signal containing aromatic residues. J. Cell Biol. 121:1197-1209.
    • (1993) J. Cell Biol. , vol.121 , pp. 1197-1209
    • Nothwehr, S.F.1    Roberts, C.J.2    Stevens, T.H.3
  • 35
    • 0027489133 scopus 로고
    • Sorting of membrane proteins in the secretory pathway
    • Pelham, H. R. B., and S. Munro. 1993. Sorting of membrane proteins in the secretory pathway. Cell 75:603-605.
    • (1993) Cell , vol.75 , pp. 603-605
    • Pelham, H.R.B.1    Munro, S.2
  • 36
    • 0029874913 scopus 로고    scopus 로고
    • Phenotypes of Bacillus subtilis mutants lacking multiple class A high-molecular weight penicillin-binding proteins
    • Popham, D. L., and P. Setlow. 1996. Phenotypes of Bacillus subtilis mutants lacking multiple class A high-molecular weight penicillin-binding proteins. J. Bacteriol. 178:2079-2089.
    • (1996) J. Bacteriol. , vol.178 , pp. 2079-2089
    • Popham, D.L.1    Setlow, P.2
  • 38
    • 0022551209 scopus 로고
    • Heterologous transmembrane and cytoplasmic domains direct functional chimeric influenza virus hemagglutinins into the endocytotic pathway
    • Roth, M. G., C. Doyle, J. Sambrook, and M. J. Gething. 1986. Heterologous transmembrane and cytoplasmic domains direct functional chimeric influenza virus hemagglutinins into the endocytotic pathway. J. Cell Biol. 102: 1271-1283.
    • (1986) J. Cell Biol. , vol.102 , pp. 1271-1283
    • Roth, M.G.1    Doyle, C.2    Sambrook, J.3    Gething, M.J.4
  • 40
    • 0028349810 scopus 로고
    • An N-terminal double-arginine motif maintains type II membrane proteins in the endoplasmic reticulum
    • Schutze, M.-P., P. A. Peterson, and M. R. Jackson. 1994. An N-terminal double-arginine motif maintains type II membrane proteins in the endoplasmic reticulum. EMBO J. 13:1696-1705.
    • (1994) EMBO J. , vol.13 , pp. 1696-1705
    • Schutze, M.-P.1    Peterson, P.A.2    Jackson, M.R.3
  • 41
    • 0024040909 scopus 로고
    • Penicillin-binding proteins of gram-negative bacteria
    • Spratt, B. G., and K. D. Cromie. 1988. Penicillin-binding proteins of gram-negative bacteria. Rev. Infect. Dis. 10:699-710.
    • (1988) Rev. Infect. Dis. , vol.10 , pp. 699-710
    • Spratt, B.G.1    Cromie, K.D.2
  • 42
    • 0023974826 scopus 로고
    • An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins
    • 38a. Strauch, K. L., and J. Beckwith. 1988. An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins. Proc. Natl. Acad. Sci. USA 85:1576-1580.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1576-1580
    • Strauch, K.L.1    Beckwith, J.2
  • 43
    • 0000651660 scopus 로고
    • The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology
    • von Heijne, G. 1986. The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology. EMBO J. 5:3021-3027.
    • (1986) EMBO J. , vol.5 , pp. 3021-3027
    • Von Heijne, G.1
  • 44
    • 0024442722 scopus 로고
    • Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues
    • von Heijne, G. 1989. Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues. Nature 341:456-458.
    • (1989) Nature , vol.341 , pp. 456-458
    • Von Heijne, G.1
  • 45
    • 0026716643 scopus 로고
    • Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule
    • von Heijne, G. 1992. Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule. J. Mol. Biol. 225:487-494.
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-494
    • Von Heijne, G.1
  • 47
    • 85036492794 scopus 로고    scopus 로고
    • Weiss, D. S., and J. Beckwith. Unpublished data
    • Weiss, D. S., and J. Beckwith. Unpublished data.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.