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Homologous expression of lysA encoding diaminopimelic acid (DAP) decarboxylase reveals increased antibiotic production in Streptomyces clavuligerus.
Otur, Çigdem; Kurt-Kizildogan, Aslihan.
Afiliação
  • Otur Ç; Enzyme and Microbial Biotechnology Section, Department of Agricultural Biotechnology, Faculty of Agriculture, Ondokuz Mayis University, 55139, Samsun, Turkey.
  • Kurt-Kizildogan A; Enzyme and Microbial Biotechnology Section, Department of Agricultural Biotechnology, Faculty of Agriculture, Ondokuz Mayis University, 55139, Samsun, Turkey. aslihan.kizildogan@omu.edu.tr.
Braz J Microbiol ; 51(2): 547-556, 2020 Jun.
Article em En | MEDLINE | ID: mdl-31833007
lysA gene encoding meso-diaminopimelic acid (DAP) decarboxylase enzyme that catalyzes L-lysine biosynthesis in the aspartate pathway in Streptomyces clavuligerus was overexpressed, and its effects on cephamycin C (CephC), clavulanic acid (CA), and tunicamycin productions were investigated. Multicopy expression of lysA gene under the control of glpF promoter (glpFp) in S. clavuligerus pCOlysA led to higher expression levels ranging from 2- to 6-fold increase at both lysA gene and CephC biosynthetic gene cluster at T36 and T48 of TSBG fermentation. These results accorded well with CephC production. Thus, 1.86- and 3.14-fold higher volumetric as well as 1.26- and 1.71-fold increased specific CephC yields were recorded in S. clavuligerus pCOlysA in comparison with the wild-type and its control strain, respectively, at 48th h. Increasing the expression of lysA provided 4.3 times more tunicamycin yields in the recombinant strain. These findings suggested that lysA overexpression in S. clavuligerus made the strain more productive for CephC and tunicamycin. The results also supported the presence of complex interactions among antibiotic biosynthesis pathways in S. clavuligerus.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Streptomyces / Carboxiliases / Antibacterianos Idioma: En Revista: Braz J Microbiol Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Turquia País de publicação: Brasil

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Streptomyces / Carboxiliases / Antibacterianos Idioma: En Revista: Braz J Microbiol Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Turquia País de publicação: Brasil