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SART3 reads methylarginine-marked glycine- and arginine-rich motifs.
- Source :
-
Cell reports [Cell Rep] 2024 Jul 23; Vol. 43 (7), pp. 114459. Date of Electronic Publication: 2024 Jul 09. - Publication Year :
- 2024
-
Abstract
- Glycine- and arginine-rich (GAR) motifs, commonly found in RNA-binding and -processing proteins, can be symmetrically (SDMA) or asymmetrically (ADMA) dimethylated at the arginine residue by protein arginine methyltransferases. Arginine-methylated protein motifs are usually read by Tudor domain-containing proteins. Here, using a GFP-Trap, we identify a non-Tudor domain protein, squamous cell carcinoma antigen recognized by T cells 3 (SART3), as a reader for SDMA-marked GAR motifs. Structural analysis and mutagenesis of SART3 show that aromatic residues lining a groove between two adjacent aromatic-rich half-a-tetratricopeptide (HAT) repeat domains are essential for SART3 to recognize and bind to SDMA-marked GAR motif peptides, as well as for the interaction between SART3 and the GAR-motif-containing proteins fibrillarin and coilin. Further, we show that the loss of this reader ability affects RNA splicing. Overall, our findings broaden the range of potential SDMA readers to include HAT domains.<br />Competing Interests: Declaration of interests M.T.B. is the co-founder of EpiCypher.<br /> (Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.)
- Subjects :
- Humans
RNA-Binding Proteins metabolism
RNA-Binding Proteins chemistry
RNA-Binding Proteins genetics
Protein Binding
RNA Splicing
HEK293 Cells
Methylation
Chromosomal Proteins, Non-Histone metabolism
Chromosomal Proteins, Non-Histone chemistry
Protein-Arginine N-Methyltransferases metabolism
Protein-Arginine N-Methyltransferases chemistry
Arginine metabolism
Arginine chemistry
Glycine metabolism
Glycine chemistry
Amino Acid Motifs
Subjects
Details
- Language :
- English
- ISSN :
- 2211-1247
- Volume :
- 43
- Issue :
- 7
- Database :
- MEDLINE
- Journal :
- Cell reports
- Publication Type :
- Academic Journal
- Accession number :
- 38985674
- Full Text :
- https://doi.org/10.1016/j.celrep.2024.114459