메뉴 건너뛰기




Volumn 10, Issue 6, 2014, Pages

A Novel Peptidoglycan Binding Protein Crucial for PBP1A-Mediated Cell Wall Biogenesis in Vibrio cholerae

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; DEXTRO AMINO ACID; LIPOPROTEIN; PROTEIN LPOA; PROTEIN PBP1A; UNCLASSIFIED DRUG; AMINO ACID; ANTIINFECTIVE AGENT; CEFSULODIN; PENICILLIN BINDING PROTEIN; PEPTIDOGLYCAN; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; PROTEIN BINDING;

EID: 84903456764     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1004433     Document Type: Article
Times cited : (34)

References (31)
  • 1
    • 50049104157 scopus 로고    scopus 로고
    • Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli
    • Vollmer W, Bertsche U, (2008) Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli. Biochim Biophys Acta 1778: 1714-1734.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 1714-1734
    • Vollmer, W.1    Bertsche, U.2
  • 2
    • 0023677844 scopus 로고
    • The composition of the murein of Escherichia coli
    • Glauner B, Holtje JV, Schwarz U, (1988) The composition of the murein of Escherichia coli. J Biol Chem 263: 10088-10095.
    • (1988) J Biol Chem , vol.263 , pp. 10088-10095
    • Glauner, B.1    Holtje, J.V.2    Schwarz, U.3
  • 3
    • 57749083521 scopus 로고    scopus 로고
    • Molecular organization of Gram-negative peptidoglycan
    • Gan L, Chen S, Jensen GJ, (2008) Molecular organization of Gram-negative peptidoglycan. Proc Natl Acad Sci U S A 105: 18953-18957.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 18953-18957
    • Gan, L.1    Chen, S.2    Jensen, G.J.3
  • 4
    • 77957963129 scopus 로고    scopus 로고
    • Bacterial shape: two-dimensional questions and possibilities
    • Young KD, (2010) Bacterial shape: two-dimensional questions and possibilities. Annu Rev Microbiol 64: 223-240.
    • (2010) Annu Rev Microbiol , vol.64 , pp. 223-240
    • Young, K.D.1
  • 5
    • 77953265009 scopus 로고    scopus 로고
    • Peptidoglycan crosslinking relaxation promotes Helicobacter pylori's helical shape and stomach colonization
    • Sycuro LK, Pincus Z, Gutierrez KD, Biboy J, Stern CA, et al. (2010) Peptidoglycan crosslinking relaxation promotes Helicobacter pylori's helical shape and stomach colonization. Cell 141: 822-833.
    • (2010) Cell , vol.141 , pp. 822-833
    • Sycuro, L.K.1    Pincus, Z.2    Gutierrez, K.D.3    Biboy, J.4    Stern, C.A.5
  • 6
    • 36549014280 scopus 로고    scopus 로고
    • Advantages and mechanisms of polarity and cell shape determination in Caulobacter crescentus
    • Lawler ML, Brun YV, (2007) Advantages and mechanisms of polarity and cell shape determination in Caulobacter crescentus. Curr Opin Microbiol 10: 630-637.
    • (2007) Curr Opin Microbiol , vol.10 , pp. 630-637
    • Lawler, M.L.1    Brun, Y.V.2
  • 7
    • 73649122749 scopus 로고    scopus 로고
    • An oldie but a goodie - cell wall biosynthesis as antibiotic target pathway
    • Schneider T, Sahl HG, (2010) An oldie but a goodie- cell wall biosynthesis as antibiotic target pathway. Int J Med Microbiol 300: 161-169.
    • (2010) Int J Med Microbiol , vol.300 , pp. 161-169
    • Schneider, T.1    Sahl, H.G.2
  • 8
    • 84855889658 scopus 로고    scopus 로고
    • From the regulation of peptidoglycan synthesis to bacterial growth and morphology
    • Typas A, Banzhaf M, Gross CA, Vollmer W, (2011) From the regulation of peptidoglycan synthesis to bacterial growth and morphology. Nat Rev Microbiol 10: 123-136.
    • (2011) Nat Rev Microbiol , vol.10 , pp. 123-136
    • Typas, A.1    Banzhaf, M.2    Gross, C.A.3    Vollmer, W.4
  • 9
    • 39149088656 scopus 로고    scopus 로고
    • The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis
    • Sauvage E, Kerff F, Terrak M, Ayala JA, Charlier P, (2008) The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis. FEMS Microbiol Rev 32: 234-258.
    • (2008) FEMS Microbiol Rev , vol.32 , pp. 234-258
    • Sauvage, E.1    Kerff, F.2    Terrak, M.3    Ayala, J.A.4    Charlier, P.5
  • 10
    • 0021862671 scopus 로고
    • Dispensability of either penicillin-binding protein-1a or -1b involved in the essential process for cell elongation in Escherichia coli
    • Kato J, Suzuki H, Hirota Y, (1985) Dispensability of either penicillin-binding protein-1a or-1b involved in the essential process for cell elongation in Escherichia coli. Mol Gen Genet 200: 272-277.
    • (1985) Mol Gen Genet , vol.200 , pp. 272-277
    • Kato, J.1    Suzuki, H.2    Hirota, Y.3
  • 11
    • 0022389693 scopus 로고
    • Lysis of Escherichia coli by beta-lactam antibiotics: deletion analysis of the role of penicillin-binding proteins 1A and 1B
    • Yousif SY, Broome-Smith JK, Spratt BG, (1985) Lysis of Escherichia coli by beta-lactam antibiotics: deletion analysis of the role of penicillin-binding proteins 1A and 1B. J Gen Microbiol 131: 2839-2845.
    • (1985) J Gen Microbiol , vol.131 , pp. 2839-2845
    • Yousif, S.Y.1    Broome-Smith, J.K.2    Spratt, B.G.3
  • 13
    • 78650497005 scopus 로고    scopus 로고
    • Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases
    • Paradis-Bleau C, Markovski M, Uehara T, Lupoli TJ, Walker S, et al. (2011) Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases. Cell 143: 1110-1120.
    • (2011) Cell , vol.143 , pp. 1110-1120
    • Paradis-Bleau, C.1    Markovski, M.2    Uehara, T.3    Lupoli, T.J.4    Walker, S.5
  • 14
    • 84892141401 scopus 로고    scopus 로고
    • Lipoprotein activators stimulate Escherichia coli penicillin-binding proteins by different mechanisms
    • Lupoli TJ, Lebar MD, Markovski M, Bernhardt T, Kahne D, et al. (2013) Lipoprotein activators stimulate Escherichia coli penicillin-binding proteins by different mechanisms. J Am Chem Soc 136: 52-55.
    • (2013) J Am Chem Soc , vol.136 , pp. 52-55
    • Lupoli, T.J.1    Lebar, M.D.2    Markovski, M.3    Bernhardt, T.4    Kahne, D.5
  • 15
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli
    • Holtje JV, (1998) Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli. Microbiol Mol Biol Rev 62: 181-203.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 181-203
    • Holtje, J.V.1
  • 16
    • 84883186566 scopus 로고    scopus 로고
    • Substrate specificity of an elongation-specific peptidoglycan endopeptidase and its implications for cell wall architecture and growth of Vibrio cholerae
    • Dörr T, Cava F, Lam H, Davis BM, Waldor MK, (2013) Substrate specificity of an elongation-specific peptidoglycan endopeptidase and its implications for cell wall architecture and growth of Vibrio cholerae. Mol Microbiol 89: 949-962.
    • (2013) Mol Microbiol , vol.89 , pp. 949-962
    • Dörr, T.1    Cava, F.2    Lam, H.3    Davis, B.M.4    Waldor, M.K.5
  • 17
    • 84870185885 scopus 로고    scopus 로고
    • Three redundant murein endopeptidases catalyse an essential cleavage step in peptidoglycan synthesis of Escherichia coli K12
    • Singh SK, SaiSree L, Amrutha RN, Reddy M, (2012) Three redundant murein endopeptidases catalyse an essential cleavage step in peptidoglycan synthesis of Escherichia coli K12. Mol Microbiol 86: 1036-1051.
    • (2012) Mol Microbiol , vol.86 , pp. 1036-1051
    • Singh, S.K.1    SaiSree, L.2    Amrutha, R.N.3    Reddy, M.4
  • 18
    • 84898870132 scopus 로고    scopus 로고
    • Differential Requirement for PBP1A and PBP1B in In Vivo and In Vitro Fitness of Vibrio cholerae
    • Dörr T, Möll A, Chao MC, Lam H, Cava F, et al. (2014) Differential Requirement for PBP1A and PBP1B in In Vivo and In Vitro Fitness of Vibrio cholerae. Infect Immun 82: 2115-2124.
    • (2014) Infect Immun , vol.82 , pp. 2115-2124
    • Dörr, T.1    Möll, A.2    Chao, M.C.3    Lam, H.4    Cava, F.5
  • 19
    • 70349321700 scopus 로고    scopus 로고
    • D-amino acids govern stationary phase cell wall remodeling in bacteria
    • Lam H, Oh DC, Cava F, Takacs CN, Clardy J, et al. (2009) D-amino acids govern stationary phase cell wall remodeling in bacteria. Science 325: 1552-1555.
    • (2009) Science , vol.325 , pp. 1552-1555
    • Lam, H.1    Oh, D.C.2    Cava, F.3    Takacs, C.N.4    Clardy, J.5
  • 20
    • 80053614751 scopus 로고    scopus 로고
    • Distinct pathways for modification of the bacterial cell wall by non-canonical D-amino acids
    • Cava F, de Pedro MA, Lam H, Davis BM, Waldor MK, (2010) Distinct pathways for modification of the bacterial cell wall by non-canonical D-amino acids. EMBO J 30: 3442-3453.
    • (2010) EMBO J , vol.30 , pp. 3442-3453
    • Cava, F.1    de Pedro, M.A.2    Lam, H.3    Davis, B.M.4    Waldor, M.K.5
  • 21
    • 84870593406 scopus 로고    scopus 로고
    • In Situ probing of newly synthesized peptidoglycan in live bacteria with fluorescent D-amino acids
    • Kuru E, Hughes HV, Brown PJ, Hall E, Tekkam S, et al. (2012) In Situ probing of newly synthesized peptidoglycan in live bacteria with fluorescent D-amino acids. Angew Chem Int Ed Engl 51: 12519-12523.
    • (2012) Angew Chem Int Ed Engl , vol.51 , pp. 12519-12523
    • Kuru, E.1    Hughes, H.V.2    Brown, P.J.3    Hall, E.4    Tekkam, S.5
  • 22
    • 4944223117 scopus 로고    scopus 로고
    • Murein (peptidoglycan) binding property of the essential cell division protein FtsN from Escherichia coli
    • Ursinus A, van den Ent F, Brechtel S, de Pedro M, Holtje JV, et al. (2004) Murein (peptidoglycan) binding property of the essential cell division protein FtsN from Escherichia coli. J Bacteriol 186: 6728-6737.
    • (2004) J Bacteriol , vol.186 , pp. 6728-6737
    • Ursinus, A.1    van den Ent, F.2    Brechtel, S.3    de Pedro, M.4    Holtje, J.V.5
  • 25
    • 0026411101 scopus 로고
    • Construction of an eae deletion mutant of enteropathogenic Escherichia coli by using a positive-selection suicide vector
    • Donnenberg MS, Kaper JB, (1991) Construction of an eae deletion mutant of enteropathogenic Escherichia coli by using a positive-selection suicide vector. Infect Immun 59: 4310-4317.
    • (1991) Infect Immun , vol.59 , pp. 4310-4317
    • Donnenberg, M.S.1    Kaper, J.B.2
  • 27
    • 47249101480 scopus 로고    scopus 로고
    • A defined transposon mutant library and its use in identifying motility genes in Vibrio cholerae
    • Cameron DE, Urbach JM, Mekalanos JJ, (2008) A defined transposon mutant library and its use in identifying motility genes in Vibrio cholerae. Proc Natl Acad Sci U S A 105: 8736-8741.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 8736-8741
    • Cameron, D.E.1    Urbach, J.M.2    Mekalanos, J.J.3
  • 28
    • 84879502179 scopus 로고    scopus 로고
    • Peptidoglycan at its peaks: how chromatographic analyses can reveal bacterial cell wall structure and assembly
    • Desmarais SM, De Pedro MA, Cava F, Huang KC, (2013) Peptidoglycan at its peaks: how chromatographic analyses can reveal bacterial cell wall structure and assembly. Mol Microbiol 89: 1-13.
    • (2013) Mol Microbiol , vol.89 , pp. 1-13
    • Desmarais, S.M.1    De Pedro, M.A.2    Cava, F.3    Huang, K.C.4
  • 29
    • 70449195156 scopus 로고
    • Reaction of ninhydrin in acid solution with straight-chain amino acids containing two amino groups and its application to the estimation of alpha epsilon-diaminopimelic acid
    • Work E, (1957) Reaction of ninhydrin in acid solution with straight-chain amino acids containing two amino groups and its application to the estimation of alpha epsilon-diaminopimelic acid. Biochem J 67: 416-423.
    • (1957) Biochem J , vol.67 , pp. 416-423
    • Work, E.1
  • 30
    • 0032510783 scopus 로고    scopus 로고
    • A bacterial two-hybrid system based on a reconstituted signal transduction pathway
    • Karimova G, Pidoux J, Ullmann A, Ladant D, (1998) A bacterial two-hybrid system based on a reconstituted signal transduction pathway. Proc Natl Acad Sci U S A 95: 5752-5756.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 5752-5756
    • Karimova, G.1    Pidoux, J.2    Ullmann, A.3    Ladant, D.4
  • 31
    • 77953996215 scopus 로고    scopus 로고
    • DipM, a new factor required for peptidoglycan remodelling during cell division in Caulobacter crescentus
    • Moll A, Schlimpert S, Briegel A, Jensen GJ, Thanbichler M, (2010) DipM, a new factor required for peptidoglycan remodelling during cell division in Caulobacter crescentus. Mol Microbiol 77: 90-107.
    • (2010) Mol Microbiol , vol.77 , pp. 90-107
    • Moll, A.1    Schlimpert, S.2    Briegel, A.3    Jensen, G.J.4    Thanbichler, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.