Abstract
BackgroundRibosome 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.ResultsIn 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.ConclusionThese 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.
Highlights
IntroductionMore than 90% of energy is used in protein synthesis [1]. A large amount of them is used in ribosome assembly and protein translation
In bacteria, more than 90% of energy is used in protein synthesis [1]
Gene organization demonstrates that SCO5703 is flanked by genes similar to those found in E. coli, including the transcription elongation factor gene nusA, the translation initiation factor gene infB, the ribosome binding factor gene rbfA and the tRNA
Summary
More than 90% of energy is used in protein synthesis [1]. A large amount of them is used in ribosome assembly and protein translation. In vitro experiments have revealed that 50S and 30S ribosomal subunits could be reconstituted into active ribosomes from isolated components through heat-activation steps under different magnesium concentrations. These steps are not required and auxiliary proteins are needed in vivo [2]. Ribosome assembly cofactor RimP is one of the auxiliary proteins required for maturation of the 30S subunit in Escherichia coli. 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
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