ArticleGenes & development2004
Arginine methyltransferase affects interactions and recruitment of mRNA processing and export factors.
Article in Genes & development, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
71 citing papers in PubMed, 133 citations in OpenAlex.
- Live-cell single-molecule dynamics of eukaryotic RNA polymerase machineries.Science (New York, N.Y.) · 2026Article
- A time-resolved framework for the recruitment of mRNP processing and assembly factors to a site of transcription.Nucleic acids research · 2025Article
- Defenders of the Transcriptome: Guard Protein-Mediated mRNA Quality Control inInternational journal of molecular sciences · 2024Review
- Homeostasis of mRNA concentrations through coupling transcription, export, and degradation.iScience · 2024Article
- Single-molecule quantitation of RNA-binding protein occupancy and stoichiometry defines a role for Yra1 (Aly/REF) in nuclear mRNP organization.Cell reports · 2023Article
- A Protein-Protein Interaction Analysis Suggests a Wide Range of New Functions for the p21-Activated Kinase (PAK) Ste20.International journal of molecular sciences · 2023Article
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- The RGG motif proteins: Interactions, functions, and regulations.Wiley interdisciplinary reviews. RNA · 2023Review
- FXR1 can bind with the CFIm25/CFIm68 complex and promote the progression of urothelial carcinoma of the bladder by stabilizing TRAF1 mRNA.Cell death & disease · 2022Article
- Review
- Robust repression of tRNA gene transcription during stress requires protein arginine methylation.Life science alliance · 2019Article
- Knockout of the Hmt1p Arginine Methyltransferase inMolecular & cellular proteomics : MCP · 2018Article
- Alternative splicing of CNOT7 diversifies CCR4-NOT functions.Nucleic acids research · 2017Article
- The winding path of protein methylation research: milestones and new frontiers.Nature reviews. Molecular cell biology · 2017Review
- KDM5 lysine demethylases are involved in maintenance of 3'UTR length.Science advances · 2016Article
- Article
- Article
- pUL69 of Human Cytomegalovirus Recruits the Cellular Protein Arginine Methyltransferase 6 via a Domain That Is Crucial for mRNA Export and Efficient Viral Replication.Journal of virology · 2015Article
- PRMT1 arginine methyltransferase accumulates in cytoplasmic bodies that respond to selective inhibition and DNA damage.European journal of histochemistry : EJH · 2014Article
- Diamidine compounds for selective inhibition of protein arginine methyltransferase 1.Journal of medicinal chemistry · 2014Article
11 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Hmt1 is the major type I arginine methyltransferase in the yeast Saccharomyces cerevisiae and facilitates the nucleocytoplasmic transport of mRNA-binding proteins through their methylation. Here we demonstrate that Hmt1 is recruited during the beginning of the transcriptional elongation process. Hmt1 methylates Yra1 and Hrp1, two mRNA-binding proteins important for mRNA processing and export. Moreover, loss of Hmt1 affects interactions between mRNA-binding proteins and Tho2, a component of the TREX (transcription/export) complex that is important for transcriptional elongation and recruitment of mRNA export factors. Furthermore, RNA in situ hybridization analysis demonstrates that loss of Hmt1 results in slowed release of HSP104 mRNA from the sites of transcription. Genome-wide location analysis shows that Hmt1 is bound to specific functional gene classes, many of which are also bound by Tho2 and other mRNA-processing factors. These data suggest a model whereby Hmt1 affects transcriptional elongation and, as a result, influences recruitment of RNA-processing factors.
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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.