ArticleScientific reports2017
Structural Basis for the Bidirectional Activity of Bacillus nanoRNase NrnA.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- RNA exoribonucleases in E. coli.Archives of microbiology · 2026Review
- Functional analyses of bacterial NanoRNase B proteins reveals defining features of this enzyme family.Nucleic acids research · 2025Article
- Structural and functional investigation of the DHH/DHHA1 family proteins in Deinococcus radiodurans.Nucleic acids research · 2024Article
- RNA processing by the CRISPR-associated NYN ribonuclease.The Biochemical journal · 2024Article
- Bacillus subtilis NrnB is expressed during sporulation and acts as a unique 3'-5' exonuclease.Nucleic acids research · 2023Article
- Assimilatory sulfate reduction in the marine methanogen Methanothermococcus thermolithotrophicus.Nature microbiology · 2023Article
- Nano-RNases: oligo- or dinucleases?FEMS microbiology reviews · 2022Review
- Article
- Structure and Function of Piezophilic HyperthermophilicInternational journal of molecular sciences · 2021Article
- Selective Translation of Low Abundance and Upregulated Transcripts in Halobacterium salinarum.mSystems · 2020Article
- Bacterial ribonucleases and their roles in RNA metabolism.Critical reviews in biochemistry and molecular biology · 2019Review
- The trimeric Hef-associated nuclease HAN is a 3'→5' exonuclease and is probably involved in DNA repair.Nucleic acids research · 2018Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
NanoRNAs are RNA fragments 2 to 5 nucleotides in length that are generated as byproducts of RNA degradation and abortive transcription initiation. Cells have specialized enzymes to degrade nanoRNAs, such as the DHH phosphoesterase family member NanoRNase A (NrnA). This enzyme was originally identified as a 3' → 5' exonuclease, but we show here that NrnA is bidirectional, degrading 2-5 nucleotide long RNA oligomers from the 3' end, and longer RNA substrates from the 5' end. The crystal structure of Bacillus subtilis NrnA reveals a dynamic bi-lobal architecture, with the catalytic N-terminal DHH domain linked to the substrate binding C-terminal DHHA1 domain via an extended linker. Whereas this arrangement is similar to the structure of RecJ, a 5' → 3' DHH family DNase and other DHH family nanoRNases, Bacillus NrnA has gained an extended substrate-binding patch that we posit is responsible for its 3' → 5' activity.
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Registered trials
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