ArticleJournal of microbiology (Seoul, Korea)2017
RraAS1 inhibits the ribonucleolytic activity of RNase ES by interacting with its catalytic domain in Streptomyces coelicolor.
Article in Journal of microbiology (Seoul, Korea), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 9 citations in OpenAlex.
- Translation as a regulatory hub for secondary metabolism in Streptomyces spp.Essays in biochemistry · 2026Review
- Identification of the global regulatory roles of RraA via the integrative transcriptome and proteome inmSphere · 2024Article
- Review
- Regulator of ribonuclease activity modulates the pathogenicity of Vibrio vulnificus.Journal of microbiology (Seoul, Korea) · 2021Article
- Bacterial RNA Degradosomes: Molecular Machines under Tight Control.Trends in biochemical sciences · 2020Review
- The coordinated action of RNase III and RNase G controls enolase expression in response to oxygen availability in Escherichia coli.Scientific reports · 2019Article
- RNase G controls tpiA mRNA abundance in response to oxygen availability in Escherichia coli.Journal of microbiology (Seoul, Korea) · 2019Article
- Crystal structure of Streptomyces coelicolor RraAS2, an unusual member of the RNase E inhibitor RraA protein family.Journal of microbiology (Seoul, Korea) · 2017Article
- Functional implications of hexameric assembly of RraA proteins from Vibrio vulnificus.PloS one · 2017Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RraA is a protein inhibitor of RNase E, which degrades and processes numerous RNAs in Escherichia coli. Streptomyces coelicolor also contains homologs of RNase E and RraA, RNase ES and RraAS1/RraAS2, respectively. Here, we report that, unlike other RraA homologs, RraAS1 directly interacts with the catalytic domain of RNase ES to exert its inhibitory effect. We further show that rraAS1 gene deletion in S. coelicolor results in a higher growth rate and increased production of actinorhodin and undecylprodigiosin, compared with the wild-type strain, suggesting that RraAS1-mediated regulation of RNase ES activity contributes to modulating the cellular physiology of S. coelicolor.
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Registered trials
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