ArticleNucleic acids research2022
Hydrogen-deuterium exchange mass spectrometry of Mtr4 with diverse RNAs reveals substrate-dependent dynamics and interfaces in the arch.
Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- Mapping of RNA Helicase Dynamics by HDX-MS.Methods in molecular biology (Clifton, N.J.) · 2027Article
- Unraveling the molecular mechanisms of vimentin interaction with G-quadruplex repeats.Nucleic acids research · 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
- Mass Spectrometry for Assessing Protein-Nucleic Acid Interactions.Analytical chemistry · 2023Review
- Using hydrogen-deuterium exchange mass spectrometry to characterize Mtr4 interactions with RNA.Methods in enzymology · 2022Article
- A yeast model for trichohepatoenteric syndrome suggests strong loss of Ski2 function in most causative mutations.microPublication biology · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Mtr4 is a eukaryotic RNA helicase required for RNA decay by the nuclear exosome. Previous studies have shown how RNA en route to the exosome threads through the highly conserved helicase core of Mtr4. Mtr4 also contains an arch domain, although details of potential interactions between the arch and RNA have been elusive. To understand the interaction of Saccharomyces cerevisiae Mtr4 with various RNAs, we have characterized RNA binding in solution using hydrogen-deuterium exchange mass spectrometry, and affinity and unwinding assays. We have identified RNA interactions within the helicase core that are consistent with existing structures and do not vary between tRNA, single-stranded RNA and double-stranded RNA constructs. We have also identified novel RNA interactions with a region of the arch known as the fist or KOW. These interactions are important for RNA unwinding and vary in strength depending on RNA structure and length. They account for Mtr4 discrimination between different RNAs. These interactions further drive Mtr4 to adopt a closed conformation characterized by reduced dynamics of the arch arm and intra-domain contacts between the fist and helicase core.
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Registered trials
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