ArticleNucleic acids research2012
Crystal structure of Hfq from Bacillus subtilis in complex with SELEX-derived RNA aptamer: insight into RNA-binding properties of bacterial Hfq.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed.
- The sRNA LhrC5 and Hfq post-transcriptionally regulate ferritin expression inFrontiers in microbiology · 2026Article
- Article
- Blocker-SELEX: a structure-guided strategy for developing inhibitory aptamers disrupting undruggable transcription factor interactions.Nature communications · 2024Article
- Recent Advances in Aptamer-Based Biosensors for Bacterial Detection.Biosensors · 2024Review
- Structural Insights into Protein-Aptamer Recognitions Emerged from Experimental and Computational Studies.International journal of molecular sciences · 2023Review
- Small proteins in Gram-positive bacteria.FEMS microbiology reviews · 2023Article
- Models of Hfq interactions with small non-coding RNA in Gram-negative and Gram-positive bacteria.Frontiers in cellular and infection microbiology · 2023Review
- Article
- The RNA Chaperone Protein Hfq Regulates the Characteristic Sporulation and Insecticidal Activity ofFrontiers in microbiology · 2022Article
- Compartmentalization-aided interaction screening reveals extensive high-order complexes within the SARS-CoV-2 proteome.Cell reports · 2021Article
- Article
- Impacts of Small RNAs and Their Chaperones on Bacterial Pathogenicity.Frontiers in cellular and infection microbiology · 2021Review
- Solution structure and RNA-binding of a minimal ProQ-homolog fromRNA (New York, N.Y.) · 2020Article
- Phase-separated condensate-aided enrichment of biomolecular interactions for high-throughput drug screening in test tubes.The Journal of biological chemistry · 2020Article
- Intermolecular Communication inFrontiers in molecular biosciences · 2020Review
- Structural insights into the modulatory role of the accessory protein WYL1 in the Type VI-D CRISPR-Cas system.Nucleic acids research · 2019Article
- Article
- Mycobacterium tuberculosis 6C sRNA binds multiple mRNA targets via C-rich loops independent of RNA chaperones.Nucleic acids research · 2019Article
- Hfq chaperone brings speed dating to bacterial sRNA.Wiley interdisciplinary reviews. RNA · 2018Review
- Architecture of the U6 snRNP reveals specific recognition of 3'-end processed U6 snRNA.Nature communications · 2018Article
Corrections and comments
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6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial Hfq is a protein that plays an important role in the regulation of genes in cooperation with sRNAs. Escherichia coli Hfq (EcHfq) has two or more sites that bind RNA(s) including U-rich and/or the poly(A) tail of mRNA. However, functional and structural information about Bacillus subtilis Hfq (BsHfq) including the RNA sequences that specifically bind to it remain unknown. Here, we describe RNA aptamers including fragment (AG)(3)A that are recognized by BsHfq and crystal structures of the BsHfq-(AG)(3)A complex at 2.2 Å resolution. Mutational and structural studies revealed that the RNA fragment binds to the distal site, one of the two binding sites on Hfq, and identified amino acid residues that are critical for sequence-specific interactions between BsHfq and (AG)(3)A. In particular, R32 appears to interact with G bases in (AG)(3)A. Poly(A) also binds to the distal site of EcHfq, but the overall RNA structure and protein-RNA interaction patterns engaged in the R32 residues of BsHfq-(AG)(3)A differ from those of EcHfq-poly(A). These findings provide novel insight into how the Hfq homologue recognizes RNA.
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