ArticleNucleic acids research2013
Characterization of MicA interactions suggests a potential novel means of gene regulation by small non-coding RNAs.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- Role of Small Non-Coding RNA in Gram-Negative Bacteria: New Insights and Comprehensive Review of Mechanisms, Functions, and Potential Applications.Molecular biotechnology · 2025Review
- DLRAPom: a hybrid pipeline of Optimized XGBoost-guided integrative multiomics analysis for identifying targetable disease-related lncRNA-miRNA-mRNA regulatory axes.Briefings in bioinformatics · 2022Article
- RNA-Binding Proteins Driving the Regulatory Activity of Small Non-coding RNAs in Bacteria.Frontiers in molecular biosciences · 2020Review
- Streptococcus sanguinis NoncodingInfection and immunity · 2018Article
- Identification of Plasmid-Encoded sRNAs in aFrontiers in microbiology · 2018Article
- The small RNA, SdsR, acts as a novel type of toxin in Escherichia coli.RNA biology · 2018Article
- Nucleoid and cytoplasmic localization of small RNAs in Escherichia coli.Nucleic acids research · 2017Article
- Experimental approaches to identify small RNAs and their diverse roles in bacteria--what we have learnt in one decade of MicA research.MicrobiologyOpen · 2015Review
- Hfq binding changes the structure ofRNA (New York, N.Y.) · 2013Article
- An improved method for surface immobilisation of RNA: application to small non-coding RNA-mRNA pairing.PloS one · 2013Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
MicA is a small non-coding RNA that regulates ompA mRNA translation in Escherichia coli. MicA has an inhibitory function, base pairing to the translation initiation region of target mRNAs through short sequences of complementarity, blocking their ribosome-binding sites. The MicA structure contains two stem loops, which impede its interaction with target mRNAs, and it is thought that the RNA chaperone protein Hfq, known to be involved in MicA regulation of ompA, may structurally remodel MicA to reveal the ompA-binding site for cognate pairing. To further characterize these interactions, we undertook biochemical and biophysical studies using native MicA and a 'stabilized' version, modified to mimic the conformational state of MicA where the ompA-binding site is exposed. Our data corroborate two proposed roles for Hfq: first, to bring both MicA and ompA into close proximity, and second, to restructure MicA to allow exposure of the ompA-binding site for pairing, thereby demonstrating the RNA chaperone function of Hfq. Additionally, at accumulated MicA levels, we identified a Mg(2+)-dependent self-association that occludes the ompA-recognition region. We discuss the potential contribution of an Mg(2+)-mediated conformational switch of MicA for the regulation of MicA function.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.