ArticleRNA biology
N. meningitidis 1681 is a member of the FinO family of RNA chaperones.
Article in RNA biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 31 citations in OpenAlex.
- 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
- The FinO/ProQ-like protein PA2582 impacts antimicrobial resistance inFrontiers in microbiology · 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
- Structural basis for recognition of transcriptional terminator structures by ProQ/FinO domain RNA chaperones.Nature communications · 2022Article
- Saturation mutagenesis charts the functional landscape of Salmonella ProQ and reveals a gene regulatory function of its C-terminal domain.Nucleic acids research · 2021Article
- In vivo targets of Salmonella FinO include a FinP-like small RNA controlling copy number of a cohabitating plasmid.Nucleic acids research · 2021Article
- The World of Stable Ribonucleoproteins and Its Mapping With Grad-Seq and Related Approaches.Frontiers in molecular biosciences · 2021Review
- Solution structure and RNA-binding of a minimal ProQ-homolog fromRNA (New York, N.Y.) · 2020Article
- Determinants of RNA recognition by the FinO domain of the Escherichia coli ProQ protein.Nucleic acids research · 2020Article
- The minimal meningococcal ProQ protein has an intrinsic capacity for structure-based global RNA recognition.Nature communications · 2020Article
- Genetic identification of the functional surface for RNA binding by Escherichia coli ProQ.Nucleic acids research · 2020Article
- The primary transcriptome of Neisseria meningitidis and its interaction with the RNA chaperone Hfq.Nucleic acids research · 2017Article
- ProQ/FinO-domain proteins: another ubiquitous family of RNA matchmakers?Molecular microbiology · 2017Review
- Structure of theRNA (New York, N.Y.) · 2017Article
- Molecular mechanism of mRNA repression inThe EMBO journal · 2017Article
- RNA-binding proteins involved in post-transcriptional regulation in bacteria.Frontiers in microbiology · 2015Review
- Biological significance of 5S rRNA import into human mitochondria: role of ribosomal protein MRP-L18.Genes & development · 2011Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The conjugative transfer of F-like plasmids between bacteria is regulated by the plasmid-encoded RNA chaperone, FinO, which facilitates sense - antisense RNA interactions to regulate plasmid gene expression. FinO was thought to adopt a unique structure, however many putative homologs have been identified in microbial genomes and are considered members of the FinO_conjugation_repressor superfamily. We were interested in determining whether other members were also able to bind RNA and promote duplex formation, suggesting that this motif does indeed identify a putative RNA chaperone. We determined the crystal structure of the N. meningitidis MC58 protein NMB1681. It revealed striking similarity to FinO, with a conserved fold and a large, positively charged surface that could function in RNA interactions. Using assays developed to study FinO-FinP sRNA interactions, NMB1681, like FinO, bound tightly to FinP RNA stem-loops with short 5' and 3' single-stranded tails but not to ssRNA. It also was able to catalyze strand exchange between an RNA duplex and a complementary single-strand, and facilitated duplexing between complementary RNA hairpins. Finally, NMB1681 was able to rescue a finO deficiency and repress F plasmid conjugation. This study strongly suggests that NMB1681 is a FinO-like RNA chaperone that likely regulates gene expression through RNA-based mechanisms in N. meningitidis.
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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.