메뉴 건너뛰기




Volumn 143, Issue 7, 1997, Pages 2295-2303

Role of the colicin A lysis protein in the expression of the colicin A operon

Author keywords

Colicin; Colicin lysis protein; Escherichia coli; Globomycin; Heat shock protein

Indexed keywords

AZIDE; BACTERIAL PROTEIN; COLICIN A; GLOBOMYCIN;

EID: 0030789030     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-143-7-2295     Document Type: Article
Times cited : (5)

References (26)
  • 1
    • 0029764787 scopus 로고    scopus 로고
    • Two beginnings for a single purpose: The dual-start holins in the regulation of phage lysis
    • Bläsi, U. & Young, R. (1996). Two beginnings for a single purpose: the dual-start holins in the regulation of phage lysis. Mol Microbiol 21, 675-682.
    • (1996) Mol Microbiol , vol.21 , pp. 675-682
    • Bläsi, U.1    Young, R.2
  • 2
    • 77956860575 scopus 로고
    • Lipoproteins: Structure, function, biosynthesis and model for protein export
    • Edited by J. M. Ghuysen & R. Hakenbeck. Amsterdam: Elsevier Science
    • Braun, V. & Wu, H. C. (1994). Lipoproteins: structure, function, biosynthesis and model for protein export. In Bacterial Cell Wall, pp. 319-341. Edited by J. M. Ghuysen & R. Hakenbeck. Amsterdam: Elsevier Science.
    • (1994) Bacterial Cell Wall , pp. 319-341
    • Braun, V.1    Wu, H.C.2
  • 3
    • 0026540963 scopus 로고
    • Colicin A and colicin E1 lysis proteins differ in their dependence on secA and secY gene products
    • Cavard, D. (1992). Colicin A and colicin E1 lysis proteins differ in their dependence on secA and secY gene products. FEBS Lett 298, 84-88.
    • (1992) FEBS Lett , vol.298 , pp. 84-88
    • Cavard, D.1
  • 4
    • 0029126664 scopus 로고
    • Effects of temperature and of heat shock on the expression and action of the colicin A lysis protein
    • Cavard, D. (1995). Effects of temperature and of heat shock on the expression and action of the colicin A lysis protein. J Bacteriol 177, 5189-5192.
    • (1995) J Bacteriol , vol.177 , pp. 5189-5192
    • Cavard, D.1
  • 5
    • 0024457020 scopus 로고
    • The acylated precursor form of the colicin A lysis protein is a natural substrate of the DegP protease
    • Cavard, D., Lazdunski, C. & Howard, S. P. (1989). The acylated precursor form of the colicin A lysis protein is a natural substrate of the DegP protease. J Bacteriol 171, 6316-6322.
    • (1989) J Bacteriol , vol.171 , pp. 6316-6322
    • Cavard, D.1    Lazdunski, C.2    Howard, S.P.3
  • 6
    • 0026648033 scopus 로고
    • Anaerobic control of colicin E1 production
    • Eraso, J. M. & Weinstock, G. M. (1992). Anaerobic control of colicin E1 production. J Bacteriol 174, 5101-5109.
    • (1992) J Bacteriol , vol.174 , pp. 5101-5109
    • Eraso, J.M.1    Weinstock, G.M.2
  • 7
    • 0029935770 scopus 로고    scopus 로고
    • Increased production of colicin E1 in stationary phase
    • Eraso, J. M., Chidambaram, M. & Weinstock, G. M. (1996). Increased production of colicin E1 in stationary phase. J Bacteriol 178, 1928-1935.
    • (1996) J Bacteriol , vol.178 , pp. 1928-1935
    • Eraso, J.M.1    Chidambaram, M.2    Weinstock, G.M.3
  • 8
    • 0030026688 scopus 로고    scopus 로고
    • Genetic evidence for an activator required for induction of colicin-like bacteriocin 28b production in Serratia marcescens by DNA-damaging agents
    • Ferrer, S., Viejo, M. B., Guasch, J. F., Enfedaque, J. & Regué, M. (1996). Genetic evidence for an activator required for induction of colicin-like bacteriocin 28b production in Serratia marcescens by DNA-damaging agents. J Bacteriol 178, 951-960.
    • (1996) J Bacteriol , vol.178 , pp. 951-960
    • Ferrer, S.1    Viejo, M.B.2    Guasch, J.F.3    Enfedaque, J.4    Regué, M.5
  • 9
    • 0027296627 scopus 로고
    • Isolation and characterization of a temperature-sensitive mutant of Salmonella typhimurium defective in prolipoprotein modification
    • Gan, K., Gupta, S. D., Sankaran, K., Schmid, M. B. & Wu, H. C. (1993). Isolation and characterization of a temperature-sensitive mutant of Salmonella typhimurium defective in prolipoprotein modification. J Biol Chem 268, 16544-16550.
    • (1993) J Biol Chem , vol.268 , pp. 16544-16550
    • Gan, K.1    Gupta, S.D.2    Sankaran, K.3    Schmid, M.B.4    Wu, H.C.5
  • 10
    • 0022575728 scopus 로고
    • A molecular genetic approach to the functioning of the immunity protein to colicin A
    • Geli, V., Baty, D., Crozel, V., Morlon, J., Lloubès, R., Pattus, F. & Lazdunski, C. (1986). A molecular genetic approach to the functioning of the immunity protein to colicin A. Mol Gen Genet 202, 455-460.
    • (1986) Mol Gen Genet , vol.202 , pp. 455-460
    • Geli, V.1    Baty, D.2    Crozel, V.3    Morlon, J.4    Lloubès, R.5    Pattus, F.6    Lazdunski, C.7
  • 11
    • 0345195392 scopus 로고
    • Structure/function relationships in the signal sequence of the colicin A lysis protein
    • (NATO ASI series H65), Edited by R. James, C. Lazdunski & F. Pattus. Berlin: Springer
    • Howard, S. P. & Lindsay, L. (1992). Structure/function relationships in the signal sequence of the colicin A lysis protein. In Bacteriocins, Microcins and Lantibiotics (NATO ASI series H65), pp. 317-329. Edited by R. James, C. Lazdunski & F. Pattus. Berlin: Springer.
    • (1992) Bacteriocins, Microcins and Lantibiotics , pp. 317-329
    • Howard, S.P.1    Lindsay, L.2
  • 12
    • 0024485644 scopus 로고
    • Amino acid sequence and length requirements for assembly and function of the colicin A lysis protein
    • Howard, S. P., Cavard, D. & Lazdunski, C. (1989). Amino acid sequence and length requirements for assembly and function of the colicin A lysis protein. J Bacteriol 171, 410-418.
    • (1989) J Bacteriol , vol.171 , pp. 410-418
    • Howard, S.P.1    Cavard, D.2    Lazdunski, C.3
  • 13
    • 0019309069 scopus 로고
    • Accumulation of glyceride-containing precursor of the outer membrane lipoprotein in the cytoplasmic membrane of Escherichia coli treated with globomycin
    • Hussain, M., Ichihara, S. & Mizushima, S. (1980). Accumulation of glyceride-containing precursor of the outer membrane lipoprotein in the cytoplasmic membrane of Escherichia coli treated with globomycin. J Biol Chem 255, 3707-3712.
    • (1980) J Biol Chem , vol.255 , pp. 3707-3712
    • Hussain, M.1    Ichihara, S.2    Mizushima, S.3
  • 15
    • 0029949518 scopus 로고    scopus 로고
    • The biology of E colicins: Paradigms and paradoxes
    • James, R., Kleanthous, C. & Moore, G. R. (1996). The biology of E colicins: paradigms and paradoxes. Microbiology 142, 1569-1580.
    • (1996) Microbiology , vol.142 , pp. 1569-1580
    • James, R.1    Kleanthous, C.2    Moore, G.R.3
  • 16
    • 0342655941 scopus 로고    scopus 로고
    • The Rz1 gene product of bacteriophage λ is a lipoprotein localized in the outer membrane of Escherichia coli
    • Kedzierska, S., Wawrzynow, A. & Taylor, A. (1996). The Rz1 gene product of bacteriophage λ is a lipoprotein localized in the outer membrane of Escherichia coli. Gene 168, 1-8.
    • (1996) Gene , vol.168 , pp. 1-8
    • Kedzierska, S.1    Wawrzynow, A.2    Taylor, A.3
  • 17
    • 0021231851 scopus 로고
    • Characterization of the ColE8 plasmid, a new member of the group E colicin plasmids
    • Lawrence, G. M. P. & James, R. (1984). Characterization of the ColE8 plasmid, a new member of the group E colicin plasmids. Gene 29, 145-155.
    • (1984) Gene , vol.29 , pp. 145-155
    • Lawrence, G.M.P.1    James, R.2
  • 19
    • 0022597009 scopus 로고
    • The promoters of the genes for colicin production, release and immunity in the ColA plasmid: Effects of convergent transcription and LexA protein
    • Lloubès, R., Baty, D. & Lazdunski, C. (1986). The promoters of the genes for colicin production, release and immunity in the ColA plasmid: effects of convergent transcription and LexA protein. Nucleic Acids Res 14, 2621-2636.
    • (1986) Nucleic Acids Res , vol.14 , pp. 2621-2636
    • Lloubès, R.1    Baty, D.2    Lazdunski, C.3
  • 20
    • 0021092930 scopus 로고
    • Isolation, molecular and functional properties of the C-termmal domain of colicin A
    • Martinez, M. C., Lazdunski, C. & Pattus, F. (1983). Isolation, molecular and functional properties of the C-termmal domain of colicin A. EMBO J 2, 1501-1507.
    • (1983) EMBO J , vol.2 , pp. 1501-1507
    • Martinez, M.C.1    Lazdunski, C.2    Pattus, F.3
  • 21
    • 0025087137 scopus 로고
    • Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery
    • Oliver, D. B., Cabelli, R. J., Dolan, K. M. & Jarosik, G. P. (1990). Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery. Proc Natl Acad Sci USA 87, 8277-8231.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 8277-18231
    • Oliver, D.B.1    Cabelli, R.J.2    Dolan, K.M.3    Jarosik, G.P.4
  • 22
    • 0021548002 scopus 로고
    • The ins and outs of colicins. Part I. Production and translocation across membranes
    • Pugsley, A. P. (1984). The ins and outs of colicins. Part I. Production and translocation across membranes. Microbiol Sci 1, 168-175.
    • (1984) Microbiol Sci , vol.1 , pp. 168-175
    • Pugsley, A.P.1
  • 23
    • 0024673026 scopus 로고
    • Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature
    • Strauch, K. L., Johnson, K. & Beckwith, J. (1989). Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature. J Bacteriol 171, 2689-2696.
    • (1989) J Bacteriol , vol.171 , pp. 2689-2696
    • Strauch, K.L.1    Johnson, K.2    Beckwith, J.3
  • 24
    • 0024561953 scopus 로고
    • Temperature-dependent insertion of prolipoprotein into Escherichia coli membrane vesicles and requirements for ATP, soluble factors, and functional SecY protein for the overall translocation process
    • Tian, G., Wu, H. C., Ray, P. H. & Tai, P. C. (1989). Temperature-dependent insertion of prolipoprotein into Escherichia coli membrane vesicles and requirements for ATP, soluble factors, and functional SecY protein for the overall translocation process. J Bacteriol 171, 1987-1997.
    • (1989) J Bacteriol , vol.171 , pp. 1987-1997
    • Tian, G.1    Wu, H.C.2    Ray, P.H.3    Tai, P.C.4
  • 25
    • 84982610130 scopus 로고
    • Bacteriocin release proteins: Mode of action, structure, and biotechnological application
    • van der Wal, F., Luirink, J. & Oudega, B. (1995). Bacteriocin release proteins: mode of action, structure, and biotechnological application. FEMS Microbiol Rev 17, 381-399.
    • (1995) FEMS Microbiol Rev , vol.17 , pp. 381-399
    • Van Der Wal, F.1    Luirink, J.2    Oudega, B.3
  • 26
    • 0026800935 scopus 로고
    • Bacteriophage lysis: Mechanism and regulation
    • Young, R. (1992). Bacteriophage lysis: mechanism and regulation. Microb Ret 56, 430-481.
    • (1992) Microb Ret , vol.56 , pp. 430-481
    • Young, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.