ArticleProceedings of the National Academy of Sciences of the United States of America2010
Structure and function of the polymerase core of TRAMP, a RNA surveillance complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- 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
- Biochemical analysis of the host factor activity of ZCCHC14 in hepatitis A virus replication.Journal of virology · 2024Article
- ELM-the Eukaryotic Linear Motif resource-2024 update.Nucleic acids research · 2024Article
- Microbial Type IA Topoisomerase C-Terminal Domain Sequence Motifs, Distribution and Combination.International journal of molecular sciences · 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
- A genome-wide CRISPR screen identifies UFMylation and TRAMP-like complexes as host factors required for hepatitis A virus infection.Cell reports · 2021Article
- A tale of non-canonical tails: gene regulation by post-transcriptional RNA tailing.Nature reviews. Molecular cell biology · 2020Review
- Substrate specificity of the TRAMP nuclear surveillance complexes.Nature communications · 2020Article
- The World of Cyclic Dinucleotides in Bacterial Behavior.Molecules (Basel, Switzerland) · 2020Review
- Purification of Endogenous Tagged TRAMP4/5 and Exosome Complexes from Yeast and In Vitro Polyadenylation-Exosome Activation Assays.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Purification and Reconstitution of the S. cerevisiae TRAMP and Ski Complexes for Biochemical and Structural Studies.Methods in molecular biology (Clifton, N.J.) · 2020Article
- The multitasking polyA tail: nuclear RNA maturation, degradation and export.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Noncoding RNA Surveillance: The Ends Justify the Means.Chemical reviews · 2018Review
- RNA surveillance by the nuclear RNA exosome: mechanisms and significance.Non-coding RNA · 2018Article
- Biochemical and structural bioinformatics studies of fungal CutA nucleotidyltransferases explain their unusual specificity toward CTP and increased tendency for cytidine incorporation at the 3'-terminal positions of synthesized tails.RNA (New York, N.Y.) · 2017Article
- Multi-domain utilization by TUT4 and TUT7 in control of let-7 biogenesis.Nature structural & molecular biology · 2017Article
- Activation mode of the eukaryotic m2G10 tRNA methyltransferase Trm11 by its partner protein Trm112.Nucleic acids research · 2017Article
- Targeting RNA for processing or destruction by the eukaryotic RNA exosome and its cofactors.Genes & development · 2017Review
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3 authors.
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Abstract
The Trf4p/Air2p/Mtr4p polyadenylation (TRAMP) complex recognizes aberrant RNAs in Saccharomyces cerevisiae and targets them for degradation. A TRAMP subcomplex consisting of a noncanonical poly(A) RNA polymerase in the Pol ss superfamily of nucleotidyl transferases, Trf4p, and a zinc knuckle protein, Air2p, mediates initial substrate recognition. Trf4p and related eukaryotic poly(A) and poly(U) polymerases differ from other characterized enzymes in the Pol ss superfamily both in sequence and in the lack of recognizable nucleic acid binding motifs. Here we report, at 2.7-A resolution, the structure of Trf4p in complex with a fragment of Air2p comprising two zinc knuckle motifs. Trf4p consists of a catalytic and central domain similar in fold to those of other noncanonical Pol beta RNA polymerases, and the two zinc knuckle motifs of Air2p interact with the Trf4p central domain. The interaction surface on Trf4p is highly conserved across eukaryotes, providing evidence that the Trf4p/Air2p complex is conserved in higher eukaryotes as well as in yeast and that the TRAMP complex may also function in RNA surveillance in higher eukaryotes. We show that Air2p, and in particular sequences encompassing a zinc knuckle motif near its N terminus, modulate Trf4p activity, and we present data supporting a role for this zinc knuckle in RNA binding. Finally, we show that the RNA 3' end plays a role in substrate recognition.
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