ArticleNucleic acids research2017
Allosteric regulation of helicase core activities of the DEAD-box helicase YxiN by RNA binding to its RNA recognition motif.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Tho1 and MOS11 promote nucleic acid double-strand unwinding by facilitating DEAD-box helicase oligomerization.Nucleic acids research · 2026Article
- Molecular insights into the Drosophila piRNA pathway via systematic ReLo protein interaction screening and structure prediction.Nucleic acids research · 2025Article
- Comprehensive identification of proteins interacting with long non-coding RNA TUG1 in R-loop regulation.Journal of biochemistry · 2025Article
- Inter-domain communication in the dimeric DEAD-box helicase Hera from T. thermophilus and implications for the mechanism of RNA unwinding.Nucleic acids research · 2025Article
- Structural basis for the activation of the DEAD-box RNA helicase DbpA by the nascent ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Specific Interaction of DDX6 with an RNA Hairpin in the 3' UTR of the Dengue Virus Genome Mediates GJournal of virology · 2021Article
- DEAD-box RNA helicase Belle posttranscriptionally promotes gene expression in an ATPase activity-dependent manner.RNA (New York, N.Y.) · 2019Article
- Crystal structures of the N-terminal domain of the Staphylococcus aureus DEAD-box RNA helicase CshA and its complex with AMP.Acta crystallographica. Section F, Structural biology communications · 2018Article
- The DEAD-Box Protein CYT-19 Uses Arginine Residues in Its C-Tail To Tether RNA Substrates.Biochemistry · 2017Article
- Characterization of the mammalian DEAD-box protein DDX5 reveals functional conservation withRNA (New York, N.Y.) · 2017Article
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3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
DEAD-box proteins share a structurally similar core of two RecA-like domains (RecA_N and RecA_C) that contain the conserved motifs for ATP-dependent RNA unwinding. In many DEAD-box proteins the helicase core is flanked by ancillary domains. To understand the regulation of the DEAD-box helicase YxiN by its C-terminal RNA recognition motif (RRM), we investigated the effect of RNA binding to the RRM on its position relative to the core, and on core activities. RRM/RNA complex formation substantially shifts the RRM from a position close to the RecA_C to the proximity of RecA_N, independent of RNA contacts with the core. RNA binding to the RRM is communicated to the core, and stimulates ATP hydrolysis and RNA unwinding. The conformational space of the core depends on the identity of the RRM-bound RNA. Allosteric regulation of core activities by RNA-induced movement of ancillary domains may constitute a general regulatory mechanism of DEAD-box protein activity.
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