메뉴 건너뛰기




Volumn 18, Issue 3, 2012, Pages 222-229

Characterization of colicin M and its orthologs targeting bacterial cell wall peptidoglycan biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOCIN; BETA LACTAM ANTIBIOTIC; COLICIN M; PEPTIDOGLYCAN; PERIPLASMIC PROTEIN; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 84862024959     PISSN: 10766294     EISSN: 19318448     Source Type: Journal    
DOI: 10.1089/mdr.2011.0230     Document Type: Conference Paper
Times cited : (18)

References (46)
  • 2
    • 0035188469 scopus 로고    scopus 로고
    • Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli
    • Arié, J.P., N. Sassoon, and J.M. Betton. 2001. Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli. Mol. Microbiol. 39:199-210.
    • (2001) Mol. Microbiol. , vol.39 , pp. 199-210
    • Arié, J.P.1    Sassoon, N.2    Betton, J.M.3
  • 4
    • 66149088098 scopus 로고    scopus 로고
    • Human- and plant-pathogenic Pseudomonas species produce bacteriocins exhibiting colicin M-like hydrolase activity towards peptidoglycan precursors
    • Barreteau, H., A. Bouhss, M. Fourgeaud, J.L. Mainardi, T. Touzé, F. Gérard, D. Blanot, M. Arthur, and D. Mengin-Lecreulx. 2009. Human- and plant-pathogenic Pseudomonas species produce bacteriocins exhibiting colicin M-like hydrolase activity towards peptidoglycan precursors. J. Bacteriol. 191:3657-3664.
    • (2009) J. Bacteriol. , vol.191 , pp. 3657-3664
    • Barreteau, H.1    Bouhss, A.2    Fourgeaud, M.3    Mainardi, J.L.4    Touzé, T.5    Gérard, F.6    Blanot, D.7    Arthur, M.8    Mengin-Lecreulx, D.9
  • 10
    • 0036589164 scopus 로고    scopus 로고
    • Ton-dependent colicins and microcins: Modular design and evolution
    • Braun, V., S.I. Patzer, and K. Hantke. 2002. Ton-dependent colicins and microcins: modular design and evolution. Biochimie 84:365-380.
    • (2002) Biochimie , vol.84 , pp. 365-380
    • Braun, V.1    Patzer, S.I.2    Hantke, K.3
  • 11
    • 0015891744 scopus 로고
    • A common receptor protein for phage T5 and colicin M in the outer membrane of Escherichia coli B
    • Braun, V., K. Schaller, and H. Wolff. 1973. A common receptor protein for phage T5 and colicin M in the outer membrane of Escherichia coli B. Biochim. Biophys. Acta 323:87-97.
    • (1973) Biochim. Biophys. Acta , vol.323 , pp. 87-97
    • Braun, V.1    Schaller, K.2    Wolff, H.3
  • 12
    • 0041335630 scopus 로고    scopus 로고
    • The complete genome sequence of the Arabidopsis and tomato pathogen Pseudomonas syringae pv. tomato DC3000
    • Buell, C.R., V. Joardar, M. Lindeberg, J. Selengut, I.T. Paulsen, M.L. Gwinn, et al. 2003. The complete genome sequence of the Arabidopsis and tomato pathogen Pseudomonas syringae pv. tomato DC3000. Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 10181-10186
    • Buell, C.R.1    Joardar, V.2    Lindeberg, M.3    Selengut, J.4    Paulsen, I.T.5    Gwinn, M.L.6
  • 14
    • 33747354636 scopus 로고    scopus 로고
    • Colicin M exerts its bacteriolytic effect via enzymatic degradation of undecaprenyl phosphate-linked peptidoglycan precursors
    • El Ghachi, M., A. Bouhss, H. Barreteau, T. Touzé, G. Auger, D. Blanot, and D. Mengin-Lecreulx. 2006. Colicin M exerts its bacteriolytic effect via enzymatic degradation of undecaprenyl phosphate-linked peptidoglycan precursors. J. Biol. Chem. 281:22761-22772.
    • (2006) J. Biol. Chem. , vol.281 , pp. 22761-22772
    • El Ghachi, M.1    Bouhss, A.2    Barreteau, H.3    Touzé, T.4    Auger, G.5    Blanot, D.6    Mengin-Lecreulx, D.7
  • 15
    • 3142731370 scopus 로고    scopus 로고
    • The bacA gene of Escherichia coli encodes an undecaprenyl pyrophosphate phosphatase activity
    • El Ghachi, M., A. Bouhss, D. Blanot, and D. Mengin-Lecreulx. 2004. The bacA gene of Escherichia coli encodes an undecaprenyl pyrophosphate phosphatase activity. J. Biol. Chem. 279:30106-30113.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30106-30113
    • El Ghachi, M.1    Bouhss, A.2    Blanot, D.3    Mengin-Lecreulx, D.4
  • 16
    • 21444450859 scopus 로고    scopus 로고
    • Identification of multiple genes encoding membrane proteins with undecaprenyl pyrophosphate phosphatase (UppP) activity in Escherichia coli
    • El Ghachi, M., A. Derbise, A. Bouhss, and D. Mengin-Lecreulx. 2005. Identification of multiple genes encoding membrane proteins with undecaprenyl pyrophosphate phosphatase (UppP) activity in Escherichia coli. J. Biol. Chem. 280:18689-18695.
    • (2005) J. Biol. Chem. , vol.280 , pp. 18689-18695
    • El Ghachi, M.1    Derbise, A.2    Bouhss, A.3    Mengin-Lecreulx, D.4
  • 17
    • 0018759646 scopus 로고
    • Mode of action of pesticin: N-acetylglucosaminidase activity
    • Ferber, D.M., and R.R. Brubaker. 1979. Mode of action of pesticin: N-acetylglucosaminidase activity. J. Bacteriol. 139:495-501.
    • (1979) J. Bacteriol. , vol.139 , pp. 495-501
    • Ferber, D.M.1    Brubaker, R.R.2
  • 19
    • 0030007664 scopus 로고    scopus 로고
    • Colicin M is inactivated during import by its immunity protein
    • Gross, P., and V. Braun. 1996. Colicin M is inactivated during import by its immunity protein. Mol. Gen. Genet. 251:388-396.
    • (1996) Mol. Gen. Genet. , vol.251 , pp. 388-396
    • Gross, P.1    Braun, V.2
  • 20
    • 0024520998 scopus 로고
    • Colicin M inhibits peptidoglycan biosynthesis by interfering with lipid carrier recycling
    • Harkness, R.E., and V. Braun. 1989. Colicin M inhibits peptidoglycan biosynthesis by interfering with lipid carrier recycling. J. Biol. Chem. 264:6177-6182.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6177-6182
    • Harkness, R.E.1    Braun, V.2
  • 21
    • 0025280089 scopus 로고
    • Colicin M is only bactericidal when provided from outside the cell
    • Harkness, R.E., and V. Braun. 1990. Colicin M is only bactericidal when provided from outside the cell. Mol. Gen. Genet. 222:37-40.
    • (1990) Mol. Gen. Genet. , vol.222 , pp. 37-40
    • Harkness, R.E.1    Braun, V.2
  • 22
    • 0024433985 scopus 로고
    • Inhibition of lipopolysaccharide O-antigen synthesis by colicin M
    • Harkness, R.E., and V. Braun. 1989. Inhibition of lipopolysaccharide O-antigen synthesis by colicin M. J. Biol. Chem. 264:14716-14722.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14716-14722
    • Harkness, R.E.1    Braun, V.2
  • 23
    • 79551485286 scopus 로고    scopus 로고
    • Mapping functional domains of colicin M
    • Helbig, S., and V. Braun. 2011. Mapping functional domains of colicin M. J. Bacteriol.193:815-821.
    • (2011) J. Bacteriol. , vol.193 , pp. 815-821
    • Helbig, S.1    Braun, V.2
  • 24
    • 79953219089 scopus 로고    scopus 로고
    • Activation of colicin M by the FkpA prolyl cis-trans isomerase/chaperone
    • Helbig, S., S.I. Patzer, C. Schiene-Fischer, K. Zeth, and V. Braun. 2011. Activation of colicin M by the FkpA prolyl cis-trans isomerase/chaperone. J. Biol. Chem. 286:6280-6290.
    • (2011) J. Biol. Chem. , vol.286 , pp. 6280-6290
    • Helbig, S.1    Patzer, S.I.2    Schiene-Fischer, C.3    Zeth, K.4    Braun, V.5
  • 25
    • 47749139311 scopus 로고    scopus 로고
    • Periplasmic chaperone FkpA is essential for imported colicin M toxicity
    • Hullmann, J., S.I. Patzer, C. Romer, K. Hantke, and V. Braun. 2008. Periplasmic chaperone FkpA is essential for imported colicin M toxicity. Mol. Microbiol. 69:926-937.
    • (2008) Mol. Microbiol. , vol.69 , pp. 926-937
    • Hullmann, J.1    Patzer, S.I.2    Romer, C.3    Hantke, K.4    Braun, V.5
  • 26
    • 73949113446 scopus 로고    scopus 로고
    • Chaperone domains convert prolyl isomerases into generic catalysts of protein folding
    • Jakob, R.P., G. Zoldàk, T. Aumüller, and F.X. Schmid. 2009. Chaperone domains convert prolyl isomerases into generic catalysts of protein folding. Proc. Natl. Acad. Sci. U.S.A. 106:20282-20287.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 20282-20287
    • Jakob, R.P.1    Zoldàk, G.2    Aumüller, T.3    Schmid, F.X.4
  • 27
    • 0023221990 scopus 로고
    • Primary structure of colicin M, an inhibitor of murein biosynthesis
    • Kock, J., T. Olschlager, R.M. Kamp, and V. Braun. 1987. Primary structure of colicin M, an inhibitor of murein biosynthesis. J. Bacteriol. 169:3358-3361.
    • (1987) J. Bacteriol. , vol.169 , pp. 3358-3361
    • Kock, J.1    Olschlager, T.2    Kamp, R.M.3    Braun, V.4
  • 29
    • 0036795113 scopus 로고    scopus 로고
    • Identification of differences in genome content among phlD-positive Pseudomonas fluorescens strains by using PCR-based subtractive hybridization
    • Mavrodi, D.V., O.V. Mavrodi, B.B. McSpadden-Gardener, B.B. Landa, D.M. Weller, and L.S. Thomashow. 2002. Identification of differences in genome content among phlD-positive Pseudomonas fluorescens strains by using PCR-based subtractive hybridization. Appl. Environ. Microbiol. 68:5170-5176.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 5170-5176
    • Mavrodi, D.V.1    Mavrodi, O.V.2    McSpadden-Gardener, B.B.3    Landa, B.B.4    Weller, D.M.5    Thomashow, L.S.6
  • 30
    • 0023626122 scopus 로고
    • Sequence, expression, and localization of the immunity protein for colicin M
    • Olschlager, T., and V. Braun. 1987. Sequence, expression, and localization of the immunity protein for colicin M. J. Bacteriol. 169:4765-4769.
    • (1987) J. Bacteriol. , vol.169 , pp. 4765-4769
    • Olschlager, T.1    Braun, V.2
  • 31
    • 0025794355 scopus 로고
    • Binding of the immunity protein inactivates colicin M
    • Ölschläger, T., A. Turba, and V. Braun. 1991. Binding of the immunity protein inactivates colicin M. Mol. Microbiol. 5:1105-1111.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1105-1111
    • Ölschläger, T.1    Turba, A.2    Braun, V.3
  • 32
    • 44949258242 scopus 로고    scopus 로고
    • How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan)
    • Park, J.T., and T. Uehara. 2008. How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan). Microbiol. Mol. Biol. Rev. 72:211-227.
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 211-227
    • Park, J.T.1    Uehara, T.2
  • 35
    • 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
  • 36
    • 0021561221 scopus 로고
    • The ins and outs of colicins. Part II. Lethal action, immunity and ecological implications
    • Pugsley, A.P. 1984. The ins and outs of colicins. Part II. Lethal action, immunity and ecological implications. Microbiol. Sci. 1:203-205.
    • (1984) Microbiol. Sci. , vol.1 , pp. 203-205
    • Pugsley, A.P.1
  • 37
    • 0027495942 scopus 로고
    • Molecular mechanisms of colicin evolution
    • Riley, M.A. 1993. Molecular mechanisms of colicin evolution. Mol. Biol. Evol. 10:1380-1395.
    • (1993) Mol. Biol. Evol. , vol.10 , pp. 1380-1395
    • Riley, M.A.1
  • 38
    • 0027324050 scopus 로고
    • Positive selection for colicin diversity in bacteria
    • Riley, M.A. 1993. Positive selection for colicin diversity in bacteria. Mol. Biol. Evol. 10:1048-1059.
    • (1993) Mol. Biol. Evol. , vol.10 , pp. 1048-1059
    • Riley, M.A.1
  • 39
    • 0019523401 scopus 로고
    • Structural and functional properties of colicin M
    • Schaller, K., R. Dreher, and V. Braun. 1981. Structural and functional properties of colicin M. J. Bacteriol. 146:54-63.
    • (1981) J. Bacteriol. , vol.146 , pp. 54-63
    • Schaller, K.1    Dreher, R.2    Braun, V.3
  • 40
    • 0020366141 scopus 로고
    • Colicin M is an inhibitor of murein biosynthesis
    • Schaller, K., J.V. Höltje, and V. Braun. 1982. Colicin M is an inhibitor of murein biosynthesis. J. Bacteriol. 152:994-1000.
    • (1982) J. Bacteriol. , vol.152 , pp. 994-1000
    • Schaller, K.1    Höltje, J.V.2    Braun, V.3
  • 41
    • 0019355106 scopus 로고
    • Temperature-sensitive, colicin M-tolerant mutant of Escherichia coli
    • Schaller, K., A. Krauel, and V. Braun. 1981. Temperature-sensitive, colicin M-tolerant mutant of Escherichia coli. J. Bacteriol. 147:135-139.
    • (1981) J. Bacteriol. , vol.147 , pp. 135-139
    • Schaller, K.1    Krauel, A.2    Braun, V.3
  • 42
    • 3242890388 scopus 로고    scopus 로고
    • In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus
    • Schneider, T., M.M. Senn, B. Berger-Bächi, A. Tossi, H.G. Sahl, and I. Wiedemann. 2004. In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus. Mol. Microbiol. 53:675-685.
    • (2004) Mol. Microbiol. , vol.53 , pp. 675-685
    • Schneider, T.1    Senn, M.M.2    Berger-Bächi, B.3    Tossi, A.4    Sahl, H.G.5    Wiedemann, I.6
  • 46
    • 54449087613 scopus 로고    scopus 로고
    • Crystal structure of colicin M, a novel phosphatase specifically imported by Escherichia coli
    • Zeth, K., C. Römer, S.I. Patzer, and V. Braun. 2008. Crystal structure of colicin M, a novel phosphatase specifically imported by Escherichia coli. J. Biol. Chem. 283:25324-25331.
    • (2008) J. Biol. Chem. , vol.283 , pp. 25324-25331
    • Zeth, K.1    Römer, C.2    Patzer, S.I.3    Braun, V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.