ArticleNucleic acids research2020
Genetic identification of the functional surface for RNA binding by Escherichia coli ProQ.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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
28 citing papers in PubMed, 38 citations in OpenAlex.
- Molecular genetic characterization of bacterial KH-domain proteins.bioRxiv : the preprint server for biology · 2026Article
- Structural dependence of ProQ-mRNA interactions in live bacterial cells.Communications biology · 2025Article
- Different RNA recognition by ProQ and FinO depends on the sequence surrounding intrinsic terminator hairpins.RNA (New York, N.Y.) · 2025Article
- RNA recognition by minimal ProQ fromRNA (New York, N.Y.) · 2025Article
- ProQ prevents mRNA degradation through inhibition of poly(A) polymerase.Nucleic acids research · 2025Article
- Improved constructs for bait RNA display in a bacterial three-hybrid assay.Scientific reports · 2025Article
- Improved constructs for bait RNA display in a bacterial three-hybrid assay.bioRxiv : the preprint server for biology · 2024Article
- ProQ-dependent activation ofmSphere · 2024Article
- The FinO/ProQ-like protein PA2582 impacts antimicrobial resistance inFrontiers in microbiology · 2024Article
- Generation of single-cysteinemicroPublication biology · 2024Article
- Biochemical and genetic dissection of the RNA-binding surface of the FinO domain ofRNA (New York, N.Y.) · 2023Article
- Biochemical and genetic dissection of the RNA-binding surface of the FinO domain ofbioRxiv : the preprint server for biology · 2023Article
- FinO/ProQ-family proteins: an evolutionary perspective.Bioscience reports · 2023Review
- Antimicrobial resistance and mechanisms of epigenetic regulation.Frontiers in cellular and infection microbiology · 2023Review
- Structural basis for recognition of transcriptional terminator structures by ProQ/FinO domain RNA chaperones.Nature communications · 2022Article
- The Role and Targets of the RNA-Binding Protein ProQ in the Gram-Negative Bacterial Pathogen Pasteurella multocida.Journal of bacteriology · 2022Article
- An RNA-binding protein acts as a major post-transcriptional modulator in Bacillus anthracis.Nature communications · 2022Article
- Bacterial RNA chaperones and chaperone-like riboregulators: behind the scenes of RNA-mediated regulation of cellular metabolism.RNA biology · 2022Article
- Scanning mutagenesis of RNA-binding protein ProQ reveals a quality control role for the Lon protease.RNA (New York, N.Y.) · 2021Article
- Saturation mutagenesis charts the functional landscape of Salmonella ProQ and reveals a gene regulatory function of its C-terminal domain.Nucleic acids research · 2021Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
The FinO-domain-protein ProQ is an RNA-binding protein that has been known to play a role in osmoregulation in proteobacteria. Recently, ProQ has been shown to act as a global RNA-binding protein in Salmonella and Escherichia coli, binding to dozens of small RNAs (sRNAs) and messenger RNAs (mRNAs) to regulate mRNA-expression levels through interactions with both 5' and 3' untranslated regions (UTRs). Despite excitement around ProQ as a novel global RNA-binding protein, and its potential to serve as a matchmaking RNA chaperone, significant gaps remain in our understanding of the molecular mechanisms ProQ uses to interact with RNA. In order to apply the tools of molecular genetics to this question, we have adapted a bacterial three-hybrid (B3H) assay to detect ProQ's interactions with target RNAs. Using domain truncations, site-directed mutagenesis and an unbiased forward genetic screen, we have identified a group of highly conserved residues on ProQ's NTD as the primary face for in vivo recognition of two RNAs, and propose that the NTD structure serves as an electrostatic scaffold to recognize the shape of an RNA duplex.
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What OpenQuestion holds
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.