Structural highlights
Disease
U5S1_HUMAN Mandibulofacial dysostosis-microcephaly syndrome. The disease is caused by mutations affecting the gene represented in this entry.
Function
U5S1_HUMAN Component of the U5 snRNP and the U4/U6-U5 tri-snRNP complex required for pre-mRNA splicing. Binds GTP.
Publication Abstract from PubMed
Pre-mRNA splicing by the spliceosome requires the biogenesis and recycling of its small nuclear ribonucleoprotein (snRNP) complexes, which are consumed in each round of splicing. The human U5 snRNP is the ~1 MDa 'heart' of the spliceosome and is recycled through an unknown mechanism involving major architectural rearrangements and the dedicated chaperones CD2BP2 and TSSC4. Late steps in U5 snRNP biogenesis similarly involve these chaperones. Here we report cryo-electron microscopy structures of four human U5 snRNP-CD2BP2-TSSC4 complexes, revealing how a series of molecular events primes the U5 snRNP to generate the ~2 MDa U4/U6.U5 tri-snRNP, the largest building block of the spliceosome.
Structural basis of human U5 snRNP late biogenesis and recycling.,Riabov Bassat D, Visanpattanasin S, Vorlander MK, Fin L, Phillips AW, Plaschka C Nat Struct Mol Biol. 2024 May;31(5):747-751. doi: 10.1038/s41594-024-01243-4. , Epub 2024 Mar 11. PMID:38467876[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Riabov Bassat D, Visanpattanasin S, Vorländer MK, Fin L, Phillips AW, Plaschka C. Structural basis of human U5 snRNP late biogenesis and recycling. Nat Struct Mol Biol. 2024 May;31(5):747-751. PMID:38467876 doi:10.1038/s41594-024-01243-4
