ArticleCell discovery2015
Structural basis for Sfm1 functioning as a protein arginine methyltransferase.
Article in Cell discovery, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Molecular basis of tRNA substrate recognition and modification by the atypical SPOUT methyltransferase Trm10.Nucleic acids research · 2026Article
- Structural insight into the novel Thermus thermophilus SPOUT methyltransferase RlmR catalysing Um2552 formation in the 23S rRNA A-loop: a case of convergent evolution.Nucleic acids research · 2025Article
- Profiling the compendium of changes in Saccharomyces cerevisiae due to mutations that alter availability of the main methyl donor S-Adenosylmethionine.G3 (Bethesda, Md.) · 2024Article
- Intrafamily heterooligomerization as an emerging mechanism of methyltransferase regulation.Epigenetics & chromatin · 2024Review
- Tied up in knots: Untangling substrate recognition by the SPOUT methyltransferases.The Journal of biological chemistry · 2022Review
- TheRNA (New York, N.Y.) · 2022Article
- The CAR-mRNA Interaction Surface Is a Zipper Extension of the Ribosome A Site.International journal of molecular sciences · 2022Article
- Arginine Methylation Regulates Ribosome CAR Function.International journal of molecular sciences · 2021Article
- A Ribosome Interaction Surface Sensitive to mRNA GCN Periodicity.Biomolecules · 2020Article
- GCN sensitive protein translation in yeast.PloS one · 2020Article
- Type I and II PRMTs regulate catabolic as well as detoxifying processes in Aspergillus nidulans.Fungal genetics and biology : FG & B · 2019Article
- A Family Divided: Distinct Structural and Mechanistic Features of the SpoU-TrmD (SPOUT) Methyltransferase Superfamily.Biochemistry · 2019Article
- Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes.The Journal of biological chemistry · 2018Article
- The ribosome: A hot spot for the identification of new types of protein methyltransferases.The Journal of biological chemistry · 2018Article
- Mechanistic features of the atypical tRNA m1G9 SPOUT methyltransferase, Trm10.Nucleic acids research · 2017Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SPOUT proteins constitute one class of methyltransferases, which so far are found to exert activity mainly towards RNAs. Previously, yeast Sfm1 was predicted to contain a SPOUT domain but can methylate ribosomal protein S3. Here we report the crystal structure of Sfm1, which comprises of a typical SPOUT domain and a small C-terminal domain. The active site is similar to that of protein arginine methyltransferases but different from that of RNA methyltransferases. In addition, Sfm1 exhibits a negatively charged surface surrounding the active site unsuitable for RNA binding. Our biochemical data show that Sfm1 exists as a monomer and has high activity towards ribosomal protein S3 but no activity towards RNA. It can specifically catalyze the methylation of Arg146 of S3 and the C-terminal domain is critical for substrate binding and activity. These results together provide the structural basis for Sfm1 functioning as a PRMT for ribosomal protein S3.
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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.