ArticleJournal of microbiology (Seoul, Korea)2017
Crystal structure of Streptomyces coelicolor RraAS2, an unusual member of the RNase E inhibitor RraA protein family.
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 6 papers.
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Who cites it
6 citing papers in PubMed, 6 citations in OpenAlex.
- S267P mutation of OxyR regulator inSynthetic and systems biotechnology · 2026Article
- Relaxed Cleavage Specificity of Hyperactive Variants of Escherichia coli RNase E on RNA I.Journal of microbiology (Seoul, Korea) · 2023Article
- An oxidative metabolic pathway of 4-deoxy-L-erythro-5-hexoseulose uronic acid (DEHU) from alginate in an alginate-assimilating bacterium.Communications biology · 2021Article
- 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
- Functional implications of hexameric assembly of RraA proteins from Vibrio vulnificus.PloS one · 2017Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial ribonuclease E (RNase E) plays a crucial role in the processing and decay of RNAs. A small protein named RraA negatively regulates the activity of RNase E via protein-protein interaction in various bacteria. Recently, RraAS1 and RraAS2, which are functional homologs of RraA from Escherichia coli, were identified in the Gram-positive species Streptomyces coelicolor. RraAS1 and RraAS2 inhibit RNase ES ribonuclease activity in S. coelicolor. RraAS1 and RraAS2 have a C-terminal extension region unlike typical bacterial RraA proteins. In this study, we present the crystal structure of RraAS2, exhibiting a hexamer arranged in a dimer of trimers, consistent with size exclusion chromatographic results. Importantly, the C-terminal extension region formed a long α-helix at the junction of the neighboring subunit, which is similar to the trimeric RraA orthologs from Saccharomyces cerevisiae. Truncation of the C-terminal extension region resulted in loss of RNase ES inhibition, demonstrating its crucial role. Our findings present the first bacterial RraA that has a hexameric assembly with a C-terminal extension α-helical region, which plays an essential role in the regulation of RNase ES activity in S. coelicolor.
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