ArticleBiochemistry2010
Unique properties of the Mtr4p-poly(A) complex suggest a role in substrate targeting.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 24 citations in OpenAlex.
- The RNA helicases Dbp2 and Mtr4 regulate the expression of Xrn1-sensitive long non-coding RNAs in yeast.Frontiers in RNA research · 2023Article
- Hydrogen-deuterium exchange mass spectrometry of Mtr4 with diverse RNAs reveals substrate-dependent dynamics and interfaces in the arch.Nucleic acids research · 2022Article
- The human SKI complex regulates channeling of ribosome-bound RNA to the exosome via an intrinsic gatekeeping mechanism.Molecular cell · 2022Article
- Article
- Mycobacterium smegmatis HelY Is an RNA-Activated ATPase/dATPase and 3'-to-5' Helicase That Unwinds 3'-Tailed RNA Duplexes and RNA:DNA Hybrids.Journal of bacteriology · 2015Article
- RBM7 subunit of the NEXT complex binds U-rich sequences and targets 3'-end extended forms of snRNAs.Nucleic acids research · 2015Article
- Interaction between the RNA-dependent ATPase and poly(A) polymerase subunits of the TRAMP complex is mediated by short peptides and important for snoRNA processing.Nucleic acids research · 2015Article
- The Mtr4 ratchet helix and arch domain both function to promote RNA unwinding.Nucleic acids research · 2014Article
- Threading the barrel of the RNA exosome.Trends in biochemical sciences · 2013Review
- Ski2-like RNA helicase structures: common themes and complex assemblies.RNA biology · 2013Review
- Nuclear noncoding RNA surveillance: is the end in sight?Trends in genetics : TIG · 2012Review
- RNA unwinding by the Trf4/Air2/Mtr4 polyadenylation (TRAMP) complex.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Yeast nuclear RNA processing.World journal of biological chemistry · 2012Article
- A brief survey of mRNA surveillance.Trends in biochemical sciences · 2011Review
- Article
- Rrp6: Integrated roles in nuclear RNA metabolism and transcription termination.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Mtr4p is a DEVH-box helicase required for 3'-end processing and degradation of various nuclear RNA substrates. In particular, Mtr4p is essential for the creation of 5.8S rRNA, U4 snRNA, and some snoRNAs and for the degradation of cryptic unstable transcripts (CUTs), aberrant mRNAs, and aberrant tRNAs. Many instances of 3'-end processing require limited polyadenylation to proceed. While polyadenylation can signal degradation in species from bacteria to humans, the mechanism whereby polyadenylated substrates are delivered to the degradation machinery is unknown. Our previous work has shown that Mtr4p preferentially binds poly(A) RNA. We suspect that this preference aids in targeting polyadenylated RNAs to the exosome. In these studies, we have investigated the mechanism underlying the preference of Mtr4p for poly(A) substrates as a means of understanding how Mtr4p might facilitate targeting. Our analysis has revealed that recognition of poly(A) substrates involves sequence-specific changes in the architecture of Mtr4p-RNA complexes. Furthermore, these differences significantly affect downstream activities. In particular, homopolymeric stretches like poly(A) ineffectively stimulate the ATPase activity of Mtr4p and suppress the rate of dissociation of the Mtr4p-RNA complex. These findings indicate that the Mtr4p-poly(A) complex is unique and ideally suited for targeting key substrates to the exosome.
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What OpenQuestion holds
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.