Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln

Current Biology

Volumn 11, Issue 24, 2001, Pages 1990-1994

  Meister, Gunter ^a   Eggert, Christian ^a   Bühler, Dirk ^a   Brahms, Hero ^b   Kambach, Christian ^c   Fischer, Utz ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^b MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^c PAUL SCHERRER INSTITUTE   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0035846546     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(01)00592-9     Document Type: Article

References (16)

1. Splicing of precursors to mRNAs by the spliceosome
2. Mechanical devices of the spliceosome: Motors, clocks, springs, and things
3. Spliceosomal UsnRNP biogenesis, structure and function
4. The snRNP core assembly pathway: Identification of stable core protein heteromeric complexes and an snRNP subcore particle in vitro
5. The SMN-SIP1 complex has an essential role in spliceosomal snRNP biogenesis
6. Essential role for the tudor domain of SMN in spliceosomal U snRNP assembly: Implications for spinal muscular atrophy
7. A novel function for SMN, the spinal muscular atrophy disease gene product, in pre-mRNA splicing
8. The spinal muscular atrophy disease gene product SMN and its associated protein SIP1 are in a complex with spliceosomal snRNP proteins
9. A multiprotein complex mediates the ATP-dependent assembly of spliceosomal U snRNPs
10. SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets
11. The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylarginines, which form a major B-cell epitope for anti-Sm autoantobodies
12. Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B′ and the Sm-like protein LSm4, and their interaction with the SMN protein
13. pICln inhibits snRNP biogenesis by binding core spliceosomal proteins
14. PRMT5 (the Janus Kinase-Binding Protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins
15. Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family
16. The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity