ArticleCurrent microbiology2016
Functional Analysis of Vibrio vulnificus Orthologs of Escherichia coli RraA and RNase E.
Article in Current microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 10 citations in OpenAlex.
- Identification of the global regulatory roles of RraA via the integrative transcriptome and proteome inmSphere · 2024Article
- Regulator of ribonuclease activity modulates the pathogenicity of Vibrio vulnificus.Journal of microbiology (Seoul, Korea) · 2021Article
- Substrate-dependent effects of quaternary structure on RNase E activity.Genes & development · 2021Article
- Bacterial RNA Degradosomes: Molecular Machines under Tight Control.Trends in biochemical sciences · 2020Review
- Bdm-Mediated Regulation of Flagellar Biogenesis in Escherichia coli and Salmonella enterica Serovar Typhimurium.Current microbiology · 2017Article
- 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
- RraAS1 inhibits the ribonucleolytic activity of RNase ES by interacting with its catalytic domain in Streptomyces coelicolor.Journal of microbiology (Seoul, Korea) · 2017Article
- RraAS2 requires both scaffold domains of RNase ES for high-affinity binding and inhibitory action on the ribonucleolytic activity.Journal of microbiology (Seoul, Korea) · 2016Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RNase E plays an important role in the degradation and processing of RNA in Escherichia coli. The enzymatic activity of RNase E is controlled by the protein inhibitors RraA and RraB. The marine pathogenic bacterium Vibrio vulnificus also contains homologs of RNase E and RraA, designated as RNase EV, RraAV1, and RraAV2. Here, we report that RraAV1 actively inhibits the enzymatic activity of RNase EV in vivo and in vitro by interacting with the C-terminal domain of RNase EV. Coexpression of RraAV1 reduced ribonucleolytic activity in the cells overproducing RNase EV and consequently restored normal growth of these cells. An in vitro cleavage assay further demonstrated that RraAV1 efficiently inhibits the ribonucleolytic activity of RNase EV on BR10 + hpT, a synthetic oligonucleotide containing the RNase E cleavage site of RNA I. Our findings suggest that RraAV1 plays an active role in RNase EV-mediated RNA cleavage in V. vulnificus.
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Registered trials
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