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TitleSubstrate adaptors are flexible tethering modules that enhance substrate methylation by the arginine methyltransferase PRMT5.
Journal, issue, pagesJ Biol Chem, Vol. 301, Issue 2, Page 108165, Year 2025
Publish dateJan 8, 2025
AuthorsCyrus Y Jin / Moritz Hunkeler / Kathleen M Mulvaney / William R Sellers / Eric S Fischer /
PubMed AbstractProtein arginine methyltransferase (PRMT) 5 is an essential arginine methyltransferase responsible for the majority of cellular symmetric dimethyl-arginine marks. PRMT5 uses substrate adaptors such ...Protein arginine methyltransferase (PRMT) 5 is an essential arginine methyltransferase responsible for the majority of cellular symmetric dimethyl-arginine marks. PRMT5 uses substrate adaptors such as pICln, RIOK1, and COPR5 to recruit and methylate a wide range of substrates. Although the substrate adaptors play important roles in substrate recognition, how they direct PRMT5 activity towards specific substrates remains incompletely understood. Using biochemistry and cryogenic electron microscopy, we show that these adaptors compete for the same binding site on PRMT5. We find that substrate adaptor and substrate complexes are bound to PRMT5 through two peptide motifs, enabling these adaptors to act as flexible tethering modules to enhance substrate methylation. Taken together, our results shed structural and mechanistic light on the PRMT5 substrate adaptor function and the biochemical nature of PRMT5 interactors.
External linksJ Biol Chem / PubMed:39793893 / PubMed Central
MethodsEM (single particle)
Resolution3.06 - 3.36 Å
Structure data

47476

9e3a

EMDB-47476, PDB-9e3a:
Cryo-EM structure of PRMT5/WDR77 in complex with 6S complex (pICln PBM local refinement)
Method: EM (single particle) / Resolution: 3.36 Å

47477

9e3b

EMDB-47477, PDB-9e3b:
Cryo-EM structure of PRMT5/WDR77 in complex with 6S complex
Method: EM (single particle) / Resolution: 3.06 Å

47478

9e3c

EMDB-47478, PDB-9e3c:
Cryo-EM structure of PRMT5/WDR77 in complex with 6S complex (GRG local refine)
Method: EM (single particle) / Resolution: 3.19 Å

Chemicals

ChemComp-SFG:
SINEFUNGIN

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / PRMT5 / Methyl transferase / WDR77 / arginine

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