ArticleNucleic acids research2012
Air2p is critical for the assembly and RNA-binding of the TRAMP complex and the KOW domain of Mtr4p is crucial for exosome activation.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 49 citations in OpenAlex.
- 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
- Mtr4 RNA helicase structures and interactions.Biological chemistry · 2021Review
- Substrate specificity of the TRAMP nuclear surveillance complexes.Nature communications · 2020Article
- 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
- Intrinsic Disorder and Posttranslational Modifications: The Darker Side of the Biological Dark Matter.Frontiers in genetics · 2018Review
- Article
- RBM7 subunit of the NEXT complex binds U-rich sequences and targets 3'-end extended forms of snRNAs.Nucleic acids research · 2015Article
- Nab3 facilitates the function of the TRAMP complex in RNA processing via recruitment of Rrp6 independent of Nrd1.PLoS genetics · 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
- Efficient mRNA polyadenylation requires a ubiquitin-like domain, a zinc knuckle, and a RING finger domain, all contained in the Mpe1 protein.Molecular and cellular biology · 2014Article
- Article
- Cotranscriptional recruitment of yeast TRAMP complex to intronic sequences promotes optimal pre-mRNA splicing.Nucleic acids research · 2014Article
- Cotranscriptional recruitment of RNA exosome cofactors Rrp47p and Mpp6p and two distinct Trf-Air-Mtr4 polyadenylation (TRAMP) complexes assists the exonuclease Rrp6p in the targeting and degradation of an aberrant messenger ribonucleoprotein particle (mRNP) in yeast.The Journal of biological chemistry · 2013Article
- Interactions affected by arginine methylation in the yeast protein-protein interaction network.Molecular & cellular proteomics : MCP · 2013Article
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
Trf4/5p-Air1/2p-Mtr4p polyadenylation complex (TRAMP) is an essential component of nuclear RNA surveillance in yeast. It recognizes a variety of nuclear transcripts produced by all three RNA polymerases, adds short poly(A) tails to aberrant or unstable RNAs and activates the exosome for their degradation. Despite the advances in understanding the structural features of the isolated complex subunits or their fragments, the details of complex assembly, RNA recognition and exosome activation remain poorly understood. Here we provide the first understanding of the RNA binding mode of the complex. We show that Air2p is an RNA-binding subunit of TRAMP. We identify the zinc knuckles (ZnK) 2, 3 and 4 as the RNA-binding domains, and reveal the essentiality of ZnK4 for TRAMP4 polyadenylation activity. Furthermore, we identify Air2p as the key component of TRAMP4 assembly providing bridging between Mtr4p and Trf4p. The former is bound via the N-terminus of Air2p, while the latter is bound via ZnK5, the linker between ZnK4 and 5 and the C-terminus of the protein. Finally, we uncover the RNA binding part of the Mtr4p arch, the KOW domain, as the essential component for TRAMP-mediated exosome activation.
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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.