메뉴 건너뛰기




Volumn 192, Issue 21, 2010, Pages 5837-5840

Latency of the lipid a deacylase PagL is involved in producing a robust permeation barrier in the outer membrane of Salmonella enterica

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; ERYTHROMYCIN; FUSIDIC ACID; LIPID A; NOVOBIOCIN; PAGL PROTEIN; PSEUDOMONIC ACID; RIFAMPICIN; UNCLASSIFIED DRUG; VANCOMYCIN; ANTIINFECTIVE AGENT; BACTERIAL PROTEIN; CARBOXYLESTERASE; LIPID; OUTER MEMBRANE PROTEIN; PAGL PROTEIN, SALMONELLA TYPHIMURIUM;

EID: 78049370418     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00758-10     Document Type: Article
Times cited : (12)

References (24)
  • 1
    • 50249128194 scopus 로고    scopus 로고
    • Structural biology of membrane-intrinsic beta-barrel enzymes: Sentinels of the bacterial outer membrane
    • Bishop, R. E. 2008. Structural biology of membrane-intrinsic beta-barrel enzymes: sentinels of the bacterial outer membrane. Biochim. Biophys. Acta 1778:1881-1896.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1881-1896
    • Bishop, R.E.1
  • 2
    • 0034596969 scopus 로고    scopus 로고
    • Transfer of palmitate from phospholipids to lipid A in outer membranes of gram-negative bacteria
    • Bishop, R. E., H. S. Gibbons, T. Guina, M. S. Trent, S. I. Miller, and C. R. Raetz. 2000. Transfer of palmitate from phospholipids to lipid A in outer membranes of gram-negative bacteria. EMBO J. 19:5071-5080.
    • (2000) EMBO J. , vol.19 , pp. 5071-5080
    • Bishop, R.E.1    Gibbons, H.S.2    Guina, T.3    Trent, M.S.4    Miller, S.I.5    Raetz, C.R.6
  • 3
    • 0024601077 scopus 로고
    • A Salmonella locus that controls resistance to microbicidal proteins from phagocytic cells
    • Fields, P. I., E. A. Groisman, and F. Heffron. 1989. A Salmonella locus that controls resistance to microbicidal proteins from phagocytic cells. Science 243:1059-1062.
    • (1989) Science , vol.243 , pp. 1059-1062
    • Fields, P.I.1    Groisman, E.A.2    Heffron, F.3
  • 4
    • 0029671310 scopus 로고    scopus 로고
    • Mg2+ as an extracellular signal: Environmental regulation of Salmonella virulence
    • García Véscovi, E., F. C. Soncini, and E. A. Groisman. 1996. Mg2+ as an extracellular signal: environmental regulation of Salmonella virulence. Cell 84:165-174.
    • (1996) Cell , vol.84 , pp. 165-174
    • García Véscovi, E.1    Soncini, F.C.2    Groisman, E.A.3
  • 5
    • 0034693060 scopus 로고    scopus 로고
    • Oxygen requirement for the biosynthesis of the S-2-hydroxymyristate moiety in Salmonella typhimurium lipid a. Function of LpxO, a new Fe2+/alpha-ketoglutarate-dependent dioxygenase homologue
    • Gibbons, H. S., S. Lin, R. J. Cotter, and C. R. Raetz. 2000. Oxygen requirement for the biosynthesis of the S-2-hydroxymyristate moiety in Salmonella typhimurium lipid A. Function of LpxO, a new Fe2+/alpha- ketoglutarate-dependent dioxygenase homologue. J. Biol. Chem. 275:32940-32949.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32940-32949
    • Gibbons, H.S.1    Lin, S.2    Cotter, R.J.3    Raetz, C.R.4
  • 7
    • 0031909562 scopus 로고    scopus 로고
    • PmrA-PmrB-regulated genes necessary for 4-aminoarabinose lipid A modification and polymyxin resistance
    • Gunn, J. S., K. B. Lim, J. Krueger, K. Kim, L. Guo, M. Hackett, and S. I. Miller. 1998. PmrA-PmrB-regulated genes necessary for 4-aminoarabinose lipid A modification and polymyxin resistance. Mol. Microbiol. 27:1171-1182.
    • (1998) Mol. Microbiol. , vol.27 , pp. 1171-1182
    • Gunn, J.S.1    Lim, K.B.2    Krueger, J.3    Kim, K.4    Guo, L.5    Hackett, M.6    Miller, S.I.7
  • 8
    • 0029809576 scopus 로고    scopus 로고
    • PhoP-PhoQ activates transcription of pmrAB, encoding a two-component regulatory system involved in Salmonella typhimurium antimicrobial peptide resistance
    • Gunn, J. S., and S. I. Miller. 1996. PhoP-PhoQ activates transcription of pmrAB, encoding a two-component regulatory system involved in Salmonella typhimurium antimicrobial peptide resistance. J. Bacteriol. 178:6857-6864.
    • (1996) J. Bacteriol. , vol.178 , pp. 6857-6864
    • Gunn, J.S.1    Miller, S.I.2
  • 9
    • 0030984298 scopus 로고    scopus 로고
    • Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ
    • Guo, L., K. B. Lim, J. S. Gunn, B. Bainbridge, R. P. Darveau, M. Hackett, and S. I. Miller. 1997. Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ. Science 276:250-253.
    • (1997) Science , vol.276 , pp. 250-253
    • Guo, L.1    Lim, K.B.2    Gunn, J.S.3    Bainbridge, B.4    Darveau, R.P.5    Hackett, M.6    Miller, S.I.7
  • 10
    • 4444240880 scopus 로고    scopus 로고
    • Connecting two-component regulatory systems by a protein that protects a response regulator from dephosphorylation by its cognate sensor
    • Kato, A., and E. A. Groisman. 2004. Connecting two-component regulatory systems by a protein that protects a response regulator from dephosphorylation by its cognate sensor. Genes Dev. 18:2302-2313.
    • (2004) Genes Dev. , vol.18 , pp. 2302-2313
    • Kato, A.1    Groisman, E.A.2
  • 11
    • 34347387346 scopus 로고    scopus 로고
    • Release of the lipopolysaccharide deacylase PagL from latency compensates for a lack of lipopolysaccharide aminoarabinose modification-dependent resistance to the antimicrobial peptide polymyxin B in Salmonella enterica
    • DOI 10.1128/JB.00451-07
    • Kawasaki, K., K. China, and M. Nishijima. 2007. Release of the lipopolysaccharide deacylase PagL from latency compensates for a lack of lipopolysaccharide aminoarabinose modification-dependent resistance to the antimicrobial peptide polymyxin B in Salmonella enterica. J. Bacteriol. 189:4911-4919. (Pubitemid 47025603)
    • (2007) Journal of Bacteriology , vol.189 , Issue.13 , pp. 4911-4919
    • Kawasaki, K.1    China, K.2    Nishijima, M.3
  • 12
    • 2442544458 scopus 로고    scopus 로고
    • 3-O-deacylation of lipid A by PagL, a PhoP/PhoQ-regulated deacylase of Salmonella typhimurium, modulates signaling through Toll-like receptor 4
    • Kawasaki, K., R. K. Ernst, and S. I. Miller. 2004. 3-O-deacylation of lipid A by PagL, a PhoP/PhoQ-regulated deacylase of Salmonella typhimurium, modulates signaling through Toll-like receptor 4. J. Biol. Chem. 279:20044-20048.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20044-20048
    • Kawasaki, K.1    Ernst, R.K.2    Miller, S.I.3
  • 13
    • 15244348949 scopus 로고    scopus 로고
    • Inhibition of Salmonella enterica serovar Typhimurium lipopolysaccharide deacylation by aminoarabinose membrane modification
    • Kawasaki, K., R. K. Ernst, and S. I. Miller. 2005. Inhibition of Salmonella enterica serovar Typhimurium lipopolysaccharide deacylation by aminoarabinose membrane modification. J. Bacteriol. 187:2448-2457.
    • (2005) J. Bacteriol. , vol.187 , pp. 2448-2457
    • Kawasaki, K.1    Ernst, R.K.2    Miller, S.I.3
  • 15
    • 3042513872 scopus 로고    scopus 로고
    • The PmrA-regulated pmrC gene mediates phosphoethanolamine modification of lipid A and polymyxin resistance in Salmonella enterica
    • Lee, H., F. F. Hsu, J. Turk, and E. A. Groisman. 2004. The PmrA-regulated pmrC gene mediates phosphoethanolamine modification of lipid A and polymyxin resistance in Salmonella enterica. J. Bacteriol. 186:4124-4133.
    • (2004) J. Bacteriol. , vol.186 , pp. 4124-4133
    • Lee, H.1    Hsu, F.F.2    Turk, J.3    Groisman, E.A.4
  • 16
    • 77953287586 scopus 로고    scopus 로고
    • Mutations in the lipid A deacylase PagL which release the enzyme from its latency affect the ability of PagL to interact with lipopolysaccharide in Salmonella enterica serovar Typhimurium
    • Manabe, T., M. Kawano, and K. Kawasaki. 2010. Mutations in the lipid A deacylase PagL which release the enzyme from its latency affect the ability of PagL to interact with lipopolysaccharide in Salmonella enterica serovar Typhimurium. Biochem. Biophys. Res. Commun. 396:812-816.
    • (2010) Biochem. Biophys. Res. Commun. , vol.396 , pp. 812-816
    • Manabe, T.1    Kawano, M.2    Kawasaki, K.3
  • 17
    • 49449087315 scopus 로고    scopus 로고
    • Extracellular loops of lipid A 3-O-deacylase PagL are involved in recognition of aminoarabinose-based membrane modifications in Salmonella enterica serovar Typhimurium
    • Manabe, T., and K. Kawasaki. 2008. Extracellular loops of lipid A 3-O-deacylase PagL are involved in recognition of aminoarabinose-based membrane modifications in Salmonella enterica serovar Typhimurium. J. Bacteriol. 190:5597-5606.
    • (2008) J. Bacteriol. , vol.190 , pp. 5597-5606
    • Manabe, T.1    Kawasaki, K.2
  • 18
    • 0003582512 scopus 로고
    • A two-component regulatory system (phoP phoQ) controls Salmonella typhimurium virulence
    • Miller, S. I., A. M. Kukral, and J. J. Mekalanos. 1989. A two-component regulatory system (phoP phoQ) controls Salmonella typhimurium virulence. Proc. Natl. Acad. Sci. U. S. A. 86:5054-5058.
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 5054-5058
    • Miller, S.I.1    Kukral, A.M.2    Mekalanos, J.J.3
  • 19
    • 35048828537 scopus 로고    scopus 로고
    • PhoPQ-mediated regulation produces a more robust permeability barrier in the outer membrane of Salmonella enterica serovar Typhimurium
    • Murata, T., W. Tseng, T. Guina, S. I. Miller, and H. Nikaido. 2007. PhoPQ-mediated regulation produces a more robust permeability barrier in the outer membrane of Salmonella enterica serovar Typhimurium. J. Bacteriol. 189:7213-7222.
    • (2007) J. Bacteriol. , vol.189 , pp. 7213-7222
    • Murata, T.1    Tseng, W.2    Guina, T.3    Miller, S.I.4    Nikaido, H.5
  • 20
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido, H. 2003. Molecular basis of bacterial outer membrane permeability revisited. Microbiol. Mol. Biol. Rev. 67:593-656.
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 22
    • 0035937824 scopus 로고    scopus 로고
    • A PhoP/PhoQ-induced lipase (PagL) that catalyzes 3-O-deacylation of lipid A precursors in membranes of Salmonella typhimurium
    • Trent, M. S., W. Pabich, C. R. Raetz, and S. I. Miller. 2001. A PhoP/PhoQ-induced lipase (PagL) that catalyzes 3-O-deacylation of lipid A precursors in membranes of Salmonella typhimurium. J. Biol. Chem. 276:9083-9092.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9083-9092
    • Trent, M.S.1    Pabich, W.2    Raetz, C.R.3    Miller, S.I.4
  • 23
    • 0026802197 scopus 로고
    • Agents that increase the permeability of the outer membrane
    • Vaara, M. 1992. Agents that increase the permeability of the outer membrane. Microbiol. Rev. 56:395-411.
    • (1992) Microbiol. Rev. , vol.56 , pp. 395-411
    • Vaara, M.1
  • 24
    • 0025782890 scopus 로고
    • Construction of versatile low-copy-number vectors for cloning, sequencing and gene expression in Escherichia coli
    • Wang, R. F., and S. R. Kushner. 1991. Construction of versatile low-copy-number vectors for cloning, sequencing and gene expression in Escherichia coli. Gene 100:195-199.
    • (1991) Gene , vol.100 , pp. 195-199
    • Wang, R.F.1    Kushner, S.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.