메뉴 건너뛰기




Volumn 195, Issue 18, 2013, Pages 4129-4137

Structure of microcin B-like compounds produced by pseudomonas syringae and species specificity of their antibacterial action

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; DNA TOPOISOMERASE (ATP HYDROLYSING); MICROCIN B; UNCLASSIFIED DRUG;

EID: 84883261261     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00665-13     Document Type: Article
Times cited : (38)

References (32)
  • 3
    • 34548508225 scopus 로고    scopus 로고
    • Structural and functional diversity of microcins, gene-encoded antibacterial peptides from enterobacteria
    • Duquesne S, Petit V, Peduzzi J, Rebuffat S. 2007. Structural and functional diversity of microcins, gene-encoded antibacterial peptides from enterobacteria. J. Mol. Microbiol. Biotechnol. 13:200-209.
    • (2007) J. Mol. Microbiol. Biotechnol. , vol.13 , pp. 200-209
    • Duquesne, S.1    Petit, V.2    Peduzzi, J.3    Rebuffat, S.4
  • 8
    • 0029923954 scopus 로고    scopus 로고
    • From peptide precursors to oxazole and thiazole-containing peptide antibiotics: microcin B17 synthase
    • Li YM, Milne JC, Madison LL, Kolter R, Walsh CT. 1996. From peptide precursors to oxazole and thiazole-containing peptide antibiotics: microcin B17 synthase. Science 274:1188-1193.
    • (1996) Science , vol.274 , pp. 1188-1193
    • Li, Y.M.1    Milne, J.C.2    Madison, L.L.3    Kolter, R.4    Walsh, C.T.5
  • 9
    • 0039130745 scopus 로고    scopus 로고
    • Cofactor requirements and reconstitution of microcin B17 synthetase: a multienzyme complex that catalyzes the formation of oxazoles and thiazoles in the antibiotic microcin B17
    • Milne JC, Roy RS, Eliot AC, Kelleher NL, Wokhlu A, Nickels B, Walsh CT. 1999. Cofactor requirements and reconstitution of microcin B17 synthetase: a multienzyme complex that catalyzes the formation of oxazoles and thiazoles in the antibiotic microcin B17. Biochemistry 38:4768-4781.
    • (1999) Biochemistry , vol.38 , pp. 4768-4781
    • Milne, J.C.1    Roy, R.S.2    Eliot, A.C.3    Kelleher, N.L.4    Wokhlu, A.5    Nickels, B.6    Walsh, C.T.7
  • 10
    • 0024022450 scopus 로고
    • The export of the DNA replication inhibitor microcin B17 provides immunity for the host cell
    • Garrido MC, Herrero M, Kolter R, Moreno F. 1988. The export of the DNA replication inhibitor microcin B17 provides immunity for the host cell. EMBO J. 7:1853-1862.
    • (1988) EMBO J , vol.7 , pp. 1853-1862
    • Garrido, M.C.1    Herrero, M.2    Kolter, R.3    Moreno, F.4
  • 11
    • 0033133846 scopus 로고    scopus 로고
    • In vivo processing and antibiotic activity of microcin B17 analogs with varying ring content and altered bisheterocyclic sites
    • Sinha Roy R, Kelleher NL, Milne JC, Walsh CT. 1999. In vivo processing and antibiotic activity of microcin B17 analogs with varying ring content and altered bisheterocyclic sites. Chem. Biol. 6:305-318.
    • (1999) Chem. Biol. , vol.6 , pp. 305-318
    • Sinha Roy, R.1    Kelleher, N.L.2    Milne, J.C.3    Walsh, C.T.4
  • 12
    • 79960686713 scopus 로고    scopus 로고
    • A major portion of DNA gyrase inhibitor microcin B17 undergoes an N Opeptidyl shift during synthesis
    • Ghilarov D, Serebryakova M, Shkundina I, Severinov K. 2011. A major portion of DNA gyrase inhibitor microcin B17 undergoes an N,Opeptidyl shift during synthesis. J. Biol. Chem. 286:26308-26318.
    • (2011) J. Biol. Chem. , vol.286 , pp. 26308-26318
    • Ghilarov, D.1    Serebryakova, M.2    Shkundina, I.3    Severinov, K.4
  • 13
    • 0036267350 scopus 로고    scopus 로고
    • The highly conserved TldD and TldE proteins of Escherichia coli are involved in microcin B17 processing and in CcdA degradation
    • Allali N, Afif H, Couturier M, Van Melderen L. 2002. The highly conserved TldD and TldE proteins of Escherichia coli are involved in microcin B17 processing and in CcdA degradation. J. Bacteriol. 184:3224-3231.
    • (2002) J. Bacteriol. , vol.184 , pp. 3224-3231
    • Allali, N.1    Afif, H.2    Couturier, M.3    Van Melderen, L.4
  • 15
    • 79551533113 scopus 로고    scopus 로고
    • Genome sequence analyses of Pseudomonas savastanoi pv. glycinea and subtractive hybridization-based comparative genomics with nine pseudomonads
    • Qi M, Wang D, Bradley CA, Zhao Y. 2011. Genome sequence analyses of Pseudomonas savastanoi pv. glycinea and subtractive hybridization-based comparative genomics with nine pseudomonads. PLoS One 6:e16451.
    • (2011) PLoS One , vol.6
    • Qi, M.1    Wang, D.2    Bradley, C.A.3    Zhao, Y.4
  • 17
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U. S. A. 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 22
    • 0024546627 scopus 로고
    • DNA sequence, products, and transcriptional pattern of the genes involved in production of the DNA replication inhibitor microcin B17
    • Genilloud O, Moreno F, Kolter R. 1989. DNA sequence, products, and transcriptional pattern of the genes involved in production of the DNA replication inhibitor microcin B17. J. Bacteriol. 171:1126-1135.
    • (1989) J. Bacteriol. , vol.171 , pp. 1126-1135
    • Genilloud, O.1    Moreno, F.2    Kolter, R.3
  • 23
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension
    • Horton RM, Hunt HD, Ho SN, Pullen JK, Pease LR. 1989. Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 77:61-68.
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 24
    • 0025726701 scopus 로고
    • Probing the limits of the DNA breakagereunion domain of the Escherichia coli DNA gyrase A protein
    • Reece RJ, Maxwell A. 1991. Probing the limits of the DNA breakagereunion domain of the Escherichia coli DNA gyrase A protein. J. Biol. Chem. 266:3540-3546.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3540-3546
    • Reece, R.J.1    Maxwell, A.2
  • 26
    • 0022516452 scopus 로고
    • Identification, mapping, cloning and characterization of a gene (sbmA) required for microcin B17 action on Escherichia coli K12
    • Laviña M, Pugsley AP, Moreno F. 1986. Identification, mapping, cloning and characterization of a gene (sbmA) required for microcin B17 action on Escherichia coli K12. J. Gen. Microbiol. 132:1685-1693.
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 1685-1693
    • Laviña, M.1    Pugsley, A.P.2    Moreno, F.3
  • 27
    • 84860327909 scopus 로고    scopus 로고
    • Comparative analysis of envelope proteomes in Escherichia coli B and K-12 strains
    • Han MJ, Lee SY, Hong SH. 2012. Comparative analysis of envelope proteomes in Escherichia coli B and K-12 strains. J. Microbiol. Biotechnol. 22:470-478.
    • (2012) J. Microbiol. Biotechnol. , vol.22 , pp. 470-478
    • Han, M.J.1    Lee, S.Y.2    Hong, S.H.3
  • 28
    • 0025964113 scopus 로고
    • The peptide antibiotic microcin B17 induces double-strand cleavage of DNA mediated by E. coli DNA gyrase
    • Vizán JL, Hernández-Chico C, del Castillo I, Moreno F. 1991. The peptide antibiotic microcin B17 induces double-strand cleavage of DNA mediated by E. coli DNA gyrase. EMBO J. 10:467-476.
    • (1991) EMBO J , vol.10 , pp. 467-476
    • Vizán, J.L.1    Hernández-Chico, C.2    del Castillo, I.3    Moreno, F.4
  • 29
    • 0001265178 scopus 로고    scopus 로고
    • Mutational analysis of posttranslational heterocycle biosynthesis in the gyrase inhibitor microcin B17: distance dependence from propeptide and tolerance for substitution in a GSCG cyclizable sequence
    • Sinha Roy R, Belshaw PJ, Walsh CT. 1998. Mutational analysis of posttranslational heterocycle biosynthesis in the gyrase inhibitor microcin B17: distance dependence from propeptide and tolerance for substitution in a GSCG cyclizable sequence. Biochemistry 37:4125-4136.
    • (1998) Biochemistry , vol.37 , pp. 4125-4136
    • Sinha Roy, R.1    Belshaw, P.J.2    Walsh, C.T.3
  • 32
    • 0032126996 scopus 로고    scopus 로고
    • Kinetics and regioselectivity of peptide-to-heterocycle conversions by microcin B17 synthetase
    • Belshaw PJ, Roy RS, Kelleher NL, Walsh CT. 1998. Kinetics and regioselectivity of peptide-to-heterocycle conversions by microcin B17 synthetase. Chem. Biol. 5:373-384.
    • (1998) Chem. Biol. , vol.5 , pp. 373-384
    • Belshaw, P.J.1    Roy, R.S.2    Kelleher, N.L.3    Walsh, C.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.