ArticleRNA biology2020
Auxiliary domains of the HrpB bacterial DExH-box helicase shape its RNA preferences.
Article in RNA biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 8 citations in OpenAlex.
- Mapping of RNA Helicase Dynamics by HDX-MS.Methods in molecular biology (Clifton, N.J.) · 2027Article
- Structural insights into the N-terminal APHB domain of HrpA: mediating canonical and i-motif recognition.Nucleic acids research · 2024Article
- The enterohemorrhagic Escherichia coli insertion sequence-excision enhancer protein is a DNA polymerase with microhomology-mediated end-joining activity.Nucleic acids research · 2023Article
- Large-scale ratcheting in a bacterial DEAH/RHA-type RNA helicase that modulates antibiotics susceptibility.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
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6 authors at 1 institution in 1 country.
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Abstract
RNA helicases are fundamental players in RNA metabolism: they remodel RNA secondary structures and arrange ribonucleoprotein complexes. While DExH-box RNA helicases function in ribosome biogenesis and splicing in eukaryotes, information is scarce about bacterial homologs. HrpB is the only bacterial DExH-box protein whose structure is solved. Besides the catalytic core, HrpB possesses three accessory domains, conserved in all DExH-box helicases, plus a unique C-terminal extension (CTE). The function of these auxiliary domains remains unknown. Here, we characterize genetically and biochemically
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