Disruption of rimP-SC, encoding a ribosome assembly cofactor, markedly enhances the production of several antibiotics in Streptomyces coelicolor
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- 作者：Yuanyuan Pan (1)
Cheng Lu (1)
Hailing Dong (1)
Lingjun Yu (1)
Gang Liu (1)
Huarong Tan (1) - 关键词：rimP ; SC ; Streptomyces coelicolor ; Actinorhodin ; Calcium ; dependent antibiotics
- 刊名：Microbial Cell Factories
- 出版年：2013
- 出版时间：December 2013
- 年：2013
- 卷：12
- 期：1
- 全文大小：1,679 KB
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Cheng Lu (1)
Hailing Dong (1)
Lingjun Yu (1)
Gang Liu (1)
Huarong Tan (1)
1. Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China - ISSN：1475-2859
文摘
Background Ribosome assembly cofactor RimP is one of the auxiliary proteins required for maturation of the 30S subunit in Escherichia coli. Although RimP in protein synthesis is important, its role in secondary metabolites biosynthesis has not been reported so far. Considering the close relationship between protein synthesis and the production of secondary metabolites, the function of ribosome assembly cofactor RimP on antibiotics production was studied in Streptomyces coelicolor and Streptomyces venezuelae. Results In this study, the rimP homologue rimP-SC was identified and cloned from Streptomyces coelicolor. Disruption of rimP-SC led to enhanced production of actinorhodin and calcium-dependent antibiotics by promoting the transcription of actII-ORF4 and cdaR. Further experiments demonstrated that MetK was one of the reasons for the increment of antibiotics production. In addition, rimP-SC disruption mutant could be used as a host to produce more peptidyl nucleoside antibiotics (polyoxin or nikkomycin) than the wild-type strain. Likewise, disruption of rimP-SV of Streptomyces venezuelae also significantly stimulated jadomycin production, suggesting that enhanced antibiotics production might be widespread in many other Streptomyces species. Conclusion These results established an important relationship between ribosome assembly cofactor and secondary metabolites biosynthesis and provided an approach for yield improvement of secondary metabolites in Streptomyces.