Journal
EMBO REPORTS
Volume 8, Issue 8, Pages 756-762Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/sj.embor.7401031
Keywords
splicing; mRNA export; ASF; RRM
Categories
Funding
- BBSRC [BB/D010519/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/D010519/1] Funding Source: researchfish
- Biotechnology and Biological Sciences Research Council [BB/D010519/1] Funding Source: Medline
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The serine/arginine-rich (SR) protein splicing factor 2/alternative splicing factor (SF2/ASF) has a role in splicing, stability, export and translation of messenger RNA. Here, we present the structure of the RNA recognition motif (RRM) 2 from SF2/ASF, which has an RRM fold with a considerably extended loop 5 region, containing a two-stranded beta-sheet. The loop 5 extension places the previously identified SR protein kinase 1 docking sequence largely within the RRM fold. We show that RRM2 binds to RNA in a new way, by using a tryptophan within a conserved SWQLKD motif that resides on helix alpha 1, together with amino acids from strand beta 2 and a histidine on loop 5. The linker connecting RRM1 and RRM2 contains arginine residues, which provide a binding site for the mRNA export factor TAP, and when TAP binds to this region it displaces RNA bound to RRM2.
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