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Volumn 181, Issue 8, 1999, Pages 2379-2384

Inducing effect of diamines on transcription of the cephamycin C genes from the lat and pcbAB promoters in Nocardia lactamdurans

Author keywords

[No Author keywords available]

Indexed keywords

CADAVERINE; CEPHAMYCIN C; PUTRESCINE;

EID: 0032931611     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.8.2379-2384.1999     Document Type: Article
Times cited : (15)

References (30)
  • 1
    • 0026800606 scopus 로고
    • Penicillin and cephalosporin biosynthetic genes: Structure, organization, regulation and evolution
    • Aharonowitz, Y., G. Cohen, and J. F. Martín. 1992. Penicillin and cephalosporin biosynthetic genes: structure, organization, regulation and evolution. Annu. Rev. Microbiol. 46:461-495.
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 461-495
    • Aharonowitz, Y.1    Cohen, G.2    Martín, J.F.3
  • 2
    • 6544229829 scopus 로고
    • A study of the conditions and mechanism of the diphenylamine reaction for the colorimetric estimation of deoxyribonucleic acid
    • Burton, K. 1956. A study of the conditions and mechanism of the diphenylamine reaction for the colorimetric estimation of deoxyribonucleic acid. Biochem. J. 62:315-323.
    • (1956) Biochem. J. , vol.62 , pp. 315-323
    • Burton, K.1
  • 3
    • 0025274612 scopus 로고
    • Streptomyces promoter-probe plasmids that utilize the xy/E gene of Pseudomonas putida
    • Clayton, T. M., and M. J. Bibb. 1990. Streptomyces promoter-probe plasmids that utilize the xy/E gene of Pseudomonas putida. Nucleic Acids Res. 18:1077.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 1077
    • Clayton, T.M.1    Bibb, M.J.2
  • 4
    • 0029846299 scopus 로고    scopus 로고
    • Overexpression of the Nocardia lactamdurans α-aminoadipyl-cysteinyl-valine synthetase in Streptomyces lividans. The purified multienzyme uses cystathionine and 6-oxopiperidine 2-carboxylate as substrates for synthesis of the tripeptide
    • Coque, J. J. R., J. L. de la Fuente, P. Liras, and J. F. Martín. 1996. Overexpression of the Nocardia lactamdurans α-aminoadipyl-cysteinyl-valine synthetase in Streptomyces lividans. The purified multienzyme uses cystathionine and 6-oxopiperidine 2-carboxylate as substrates for synthesis of the tripeptide. Eur. J. Biochem. 242:264-270.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 264-270
    • Coque, J.J.R.1    De La Fuente, J.L.2    Liras, P.3    Martín, J.F.4
  • 5
    • 0025951613 scopus 로고
    • A gene encoding lysine 6-aminotransferase, which forms the β-lactam precursor α-aminoadipic acid, is located in the cluster of cephamycin biosynthetic genes in Nocardia lactamdurans
    • Coque, J. J. R., P. Liras, L. Láiz, and J. F. Martín. 1991. A gene encoding lysine 6-aminotransferase, which forms the β-lactam precursor α-aminoadipic acid, is located in the cluster of cephamycin biosynthetic genes in Nocardia lactamdurans. J. Bacteriol. 173:6258-6264.
    • (1991) J. Bacteriol. , vol.173 , pp. 6258-6264
    • Coque, J.J.R.1    Liras, P.2    Láiz, L.3    Martín, J.F.4
  • 6
    • 0027525974 scopus 로고
    • Genes for a β-lactamase, a penicillin-binding protein and a transmembrane protein are clustered with the cephamycin biosynthetic genes in Nocardia lactamdurans
    • Coque, J. J. R., P. Liras, and J. F. Martín. 1993. Genes for a β-lactamase, a penicillin-binding protein and a transmembrane protein are clustered with the cephamycin biosynthetic genes in Nocardia lactamdurans. EMBO J. 12:631-639.
    • (1993) EMBO J. , vol.12 , pp. 631-639
    • Coque, J.J.R.1    Liras, P.2    Martín, J.F.3
  • 7
    • 0025910809 scopus 로고
    • The cephamycin biosynthetic genes pcbAB, encoding a large multidomain peptide synthetase, and pcbC of Nocardia lactamdurans are clustered together in an organization different from Acremonium chrysogenum and Penicillium chrysogenum
    • Coque, J. J. R., J. F. Martín, J. G. Calzada, and P. Liras. 1991. The cephamycin biosynthetic genes pcbAB, encoding a large multidomain peptide synthetase, and pcbC of Nocardia lactamdurans are clustered together in an organization different from Acremonium chrysogenum and Penicillium chrysogenum. Mol. Microbiol. 5:1125-1133.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1125-1133
    • Coque, J.J.R.1    Martín, J.F.2    Calzada, J.G.3    Liras, P.4
  • 8
    • 0030693246 scopus 로고    scopus 로고
    • Δ-1-Piperideine-6-carboxylate dehydrogenase, a new enzyme that forms α-aminoadipate in Streptomyces clavuligerus and other cephamycin C-producing actinomycetes
    • De la Fuente, J. L., A. Rumbero, J. F. Martín, and P. Liras. 1997. Δ-1-Piperideine-6-carboxylate dehydrogenase, a new enzyme that forms α-aminoadipate in Streptomyces clavuligerus and other cephamycin C-producing actinomycetes. Biochem. J. 327:59-64.
    • (1997) Biochem. J. , vol.327 , pp. 59-64
    • De La Fuente, J.L.1    Rumbero, A.2    Martín, J.F.3    Liras, P.4
  • 9
    • 8944248272 scopus 로고    scopus 로고
    • Polyamines decrease Escherichia cou outer membrane permeability
    • De la Vega, A. L., and A. H. Delcour. 1996. Polyamines decrease Escherichia cou outer membrane permeability. J. Bacteriol. 178:3715-3721.
    • (1996) J. Bacteriol. , vol.178 , pp. 3715-3721
    • De La Vega, A.L.1    Delcour, A.H.2
  • 11
    • 0031679836 scopus 로고    scopus 로고
    • The nine genes of the Nocardia lactamdurans cephamycin cluster are transcribed into large mRNAs from three promoters, two of them located in a bidirectional promoter region
    • Enguita, F. J., J. J. R. Coque, P. Liras, and J. F. Martín. 1998. The nine genes of the Nocardia lactamdurans cephamycin cluster are transcribed into large mRNAs from three promoters, two of them located in a bidirectional promoter region. J. Bacteriol. 180:5489-5494.
    • (1998) J. Bacteriol. , vol.180 , pp. 5489-5494
    • Enguita, F.J.1    Coque, J.J.R.2    Liras, P.3    Martín, J.F.4
  • 12
    • 0030465056 scopus 로고    scopus 로고
    • Interaction of the two proteins of the methoxylation system involved in cephamycin C biosynthesis. Immunoaffinity, protein cross-linking, and fluorescence spectroscopy studies
    • Enguita, F. J., P. Liras, A. L. Leitão, and J. F. Martín. 1996. Interaction of the two proteins of the methoxylation system involved in cephamycin C biosynthesis. Immunoaffinity, protein cross-linking, and fluorescence spectroscopy studies. J. Biol. Chem. 271:33225-33230.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33225-33230
    • Enguita, F.J.1    Liras, P.2    Leitão, A.L.3    Martín, J.F.4
  • 13
    • 0018394517 scopus 로고
    • Sporulation and serine protease production by Streptomyces lactamdurans
    • Ginther, C. L. 1979. Sporulation and serine protease production by Streptomyces lactamdurans. Antimicrob. Agents Chemother. 15:522-526.
    • (1979) Antimicrob. Agents Chemother. , vol.15 , pp. 522-526
    • Ginther, C.L.1
  • 14
    • 0344191932 scopus 로고
    • August U.S, patent 3,977,942
    • Inamine, E., and J. Birnbaum. August 1976. U.S, patent 3,977,942.
    • (1976)
    • Inamine, E.1    Birnbaum, J.2
  • 15
    • 0025866196 scopus 로고
    • Polyamines as constituents of the outer membranes of Escherichia coli and Salmonella tryphimurium
    • Koshi, P., and M. Vaara. 1991. Polyamines as constituents of the outer membranes of Escherichia coli and Salmonella tryphimurium. J. Bacteriol. 173:3695-3699.
    • (1991) J. Bacteriol. , vol.173 , pp. 3695-3699
    • Koshi, P.1    Vaara, M.2
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0031549639 scopus 로고    scopus 로고
    • Improved oxygen transfer in cultures of Nocardia lactamdurans maintains the cephamycin biosynthetic proteins for prolonged times and enhances the conversion of deacetylcephalosporin into cephamycin C
    • Leitão, A. L., F. J. Enguita, and J. F. Martín. 1997. Improved oxygen transfer in cultures of Nocardia lactamdurans maintains the cephamycin biosynthetic proteins for prolonged times and enhances the conversion of deacetylcephalosporin into cephamycin C. J. Biotechnol. 58:39-50.
    • (1997) J. Biotechnol. , vol.58 , pp. 39-50
    • Leitão, A.L.1    Enguita, F.J.2    Martín, J.F.3
  • 18
    • 0030470447 scopus 로고    scopus 로고
    • Allophane increases the protein levels of several cephamycin biosynthetic enzymes in Nocardia lactamdurans
    • Leitão, A. L., F. J. Enguita, J. L. De la Fuente, P. Liras, and J. F. Martín. 1996. Allophane increases the protein levels of several cephamycin biosynthetic enzymes in Nocardia lactamdurans. Microbiology 142:3399-3406.
    • (1996) Microbiology , vol.142 , pp. 3399-3406
    • Leitão, A.L.1    Enguita, F.J.2    De La Fuente, J.L.3    Liras, P.4    Martín, J.F.5
  • 21
    • 0024486867 scopus 로고
    • Lysine catabolism in Streptomyces sp. Is primarily through cadaverine: β-lactam producers also make α-aminoadipate
    • Madduri, K., C. Stuttard, and L. C. Vining. 1989. Lysine catabolism in Streptomyces sp. is primarily through cadaverine: β-lactam producers also make α-aminoadipate. J. Bacteriol. 171:299-302.
    • (1989) J. Bacteriol. , vol.171 , pp. 299-302
    • Madduri, K.1    Stuttard, C.2    Vining, L.C.3
  • 22
    • 0031873963 scopus 로고    scopus 로고
    • New aspects of genes and enzymes for β-lactam antibiotic biosynthesis
    • Martín, J. F. 1998. New aspects of genes and enzymes for β-lactam antibiotic biosynthesis. Appl. Microbiol. Biotechnol. 50:1-15.
    • (1998) Appl. Microbiol. Biotechnol. , vol.50 , pp. 1-15
    • Martín, J.F.1
  • 23
    • 0024460765 scopus 로고
    • Organization and expression of genes involved in the biosynthesis of antibiotics and other secondary metabolites
    • Martín, J. F., and P. Liras. 1989. Organization and expression of genes involved in the biosynthesis of antibiotics and other secondary metabolites. Annu. Rev. Microbiol. 43:173-206.
    • (1989) Annu. Rev. Microbiol. , vol.43 , pp. 173-206
    • Martín, J.F.1    Liras, P.2
  • 24
    • 0021755628 scopus 로고
    • Preferential stimulation of the in vivo synthesis of a protein by polyamines in Escherichia coli: Purification and properties of the specific protein
    • Mitsui, K., K. Igarashi, T. Kakegawa, and S. Hirose. 1984. Preferential stimulation of the in vivo synthesis of a protein by polyamines in Escherichia coli: purification and properties of the specific protein. Biochemistry 23: 2679-2683.
    • (1984) Biochemistry , vol.23 , pp. 2679-2683
    • Mitsui, K.1    Igarashi, K.2    Kakegawa, T.3    Hirose, S.4
  • 25
    • 0031751106 scopus 로고    scopus 로고
    • The pcd gene encoding piperideine-6-carboxylate dehydrogenase involved in biosynthesis of α-aminoadipic acid is located in the cephamycin cluster of Streptomyces clavuligerus
    • Pérez-Llarena, F. J., A. Rodríguez-García, F. J. Enguita, J. F. Martín, and P. Liras. 1998. The pcd gene encoding piperideine-6-carboxylate dehydrogenase involved in biosynthesis of α-aminoadipic acid is located in the cephamycin cluster of Streptomyces clavuligerus. J. Bacteriol. 180:4753-4756.
    • (1998) J. Bacteriol. , vol.180 , pp. 4753-4756
    • Pérez-Llarena, F.J.1    Rodríguez-García, A.2    Enguita, F.J.3    Martín, J.F.4    Liras, P.5
  • 27
    • 0019183039 scopus 로고
    • Increase in activity of β-lactam synthetases after growth of Cephalosporium acremonium with methionine or norleucine
    • Sawada, Y., T. Konomi, N. A. Solomon, and A. L. Demain. 1980. Increase in activity of β-lactam synthetases after growth of Cephalosporium acremonium with methionine or norleucine. FEMS Microbiol, Lett. 9:281-284.
    • (1980) FEMS Microbiol, Lett. , vol.9 , pp. 281-284
    • Sawada, Y.1    Konomi, T.2    Solomon, N.A.3    Demain, A.L.4
  • 28
    • 0031928331 scopus 로고    scopus 로고
    • Characterization of polyamine synthesis pathway in Bacillus subtilis 168
    • Sekowska, A., P. Bertin, and A. Danchin. 1998. Characterization of polyamine synthesis pathway in Bacillus subtilis 168. Mol. Microbiol. 29:851-858.
    • (1998) Mol. Microbiol. , vol.29 , pp. 851-858
    • Sekowska, A.1    Bertin, P.2    Danchin, A.3
  • 30
    • 0022001625 scopus 로고
    • Polyamines in microorganisms
    • Tabor, C. W, and H. Tabor. 1985. Polyamines in microorganisms. Microbiol. Rev. 49:81-99.
    • (1985) Microbiol. Rev. , vol.49 , pp. 81-99
    • Tabor, C.W.1    Tabor, H.2


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