Affiliation:
1. MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Abstract
A human P spliceosome structure
Splicing of some pre–messenger RNAs could be regulated by cell type–specific splicing factors. Fica
et al.
describe the cryo–electron microscopy structure of the human postcatalytic (P) spliceosome. Surprisingly, it lacks the splicing factor Prp18, which plays an essential role in exon ligation in the yeast spliceosome. Instead, a metazoan-specific splicing factor, FAM32A, compensates for Prp18 and promotes exon ligation by penetrating the active sites and directly stapling the 5′ exon and the 3′ splice site. These findings suggest a way to control tissue-specific alternative splicing.
Science
, this issue p.
710
Funder
H2020 European Research Council
Medical Research Council
Publisher
American Association for the Advancement of Science (AAAS)
Cited by
85 articles.
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