ArticleNucleic acids research2014
The Mtr4 ratchet helix and arch domain both function to promote RNA unwinding.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 37 citations in OpenAlex.
- DNTTIP2 coordinates RNA exosome activities to ensure fidelity of human ribosome assembly.Nature communications · 2026Article
- N-Terminus of Cid14 Activates RNA Unwinding by Mtr4 in theBiochemistry · 2025Article
- TRAMP assembly alters the conformation and RNA binding of Mtr4 and Trf4-Air2.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Conserved Residues at the Mtr4 C-Terminus Coordinate Helicase Activity and Exosome Interactions.Biochemistry · 2024Article
- In vivo characterization of the critical interaction between the RNA exosome and the essential RNA helicase Mtr4 in Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2023Article
- Hydrogen-deuterium exchange mass spectrometry of Mtr4 with diverse RNAs reveals substrate-dependent dynamics and interfaces in the arch.Nucleic acids research · 2022Article
- Using hydrogen-deuterium exchange mass spectrometry to characterize Mtr4 interactions with RNA.Methods in enzymology · 2022Article
- Methods to assess helicase and translocation activities of human nuclear RNA exosome and RNA adaptor complexes.Methods in enzymology · 2022Article
- A yeast model for trichohepatoenteric syndrome suggests strong loss of Ski2 function in most causative mutations.microPublication biology · 2022Article
- Mtr4 RNA helicase structures and interactions.Biological chemistry · 2021Review
- Substrate discrimination and quality control require each catalytic activity of TRAMP and the nuclear RNA exosome.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- NRDE2 negatively regulates exosome functions by inhibiting MTR4 recruitment and exosome interaction.Genes & development · 2019Article
- Proteomic profiling and functional characterization of post-translational modifications of the fission yeast RNA exosome.Nucleic acids research · 2018Article
- RNA helicases in RNA decay.Biochemical Society transactions · 2018Review
- Article
- Structure of the DEAH/RHA ATPase Prp43p bound to RNA implicates a pair of hairpins and motif Va in translocation along RNA.RNA (New York, N.Y.) · 2017Article
- Targeting RNA for processing or destruction by the eukaryotic RNA exosome and its cofactors.Genes & development · 2017Review
- Functions and regulation of the Brr2 RNA helicase during splicing.Cell cycle (Georgetown, Tex.) · 2016Review
- Structure of the frequency-interacting RNA helicase: a protein interaction hub for the circadian clock.The EMBO journal · 2016Article
- Retinitis Pigmentosa Mutations in Bad Response to Refrigeration 2 (Brr2) Impair ATPase and Helicase Activity.The Journal of biological chemistry · 2016Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Mtr4 is a conserved Ski2-like RNA helicase and a subunit of the TRAMP complex that activates exosome-mediated 3'-5' turnover in nuclear RNA surveillance and processing pathways. Prominent features of the Mtr4 structure include a four-domain ring-like helicase core and a large arch domain that spans the core. The 'ratchet helix' is positioned to interact with RNA substrates as they move through the helicase. However, the contribution of the ratchet helix in Mtr4 activity is poorly understood. Here we show that strict conservation along the ratchet helix is particularly extensive for Ski2-like RNA helicases compared to related helicases. Mutation of residues along the ratchet helix alters in vitro activity in Mtr4 and TRAMP and causes slow growth phenotypes in vivo. We also identify a residue on the ratchet helix that influences Mtr4 affinity for polyadenylated substrates. Previous work indicated that deletion of the arch domain has minimal effect on Mtr4 unwinding activity. We now show that combining the arch deletion with ratchet helix mutations abolishes helicase activity and produces a lethal in vivo phenotype. These studies demonstrate that the ratchet helix modulates helicase activity and suggest that the arch domain plays a previously unrecognized role in unwinding substrates.
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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.