A human postcatalytic spliceosome structure reveals essential roles of metazoan factors for exon ligation
| Autor: | Andrew J. Newman, Chris Oubridge, Sebastian M. Fica, Kiyoshi Nagai, Max E. Wilkinson |
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| Rok vydání: | 2019 |
| Předmět: |
Spliceosome
Chromosomal Proteins Non-Histone Protein Conformation Article 03 medical and health sciences Exon 0302 clinical medicine RNA Precursors Humans 030304 developmental biology 0303 health sciences Messenger RNA Multidisciplinary Chemistry Cryoelectron Microscopy Alternative splicing Intron Nuclear Proteins RNA Exons Cell biology DNA-Binding Proteins Repressor Proteins Alternative Splicing RNA splicing Biocatalysis Spliceosomes RNA Splice Sites Carrier Proteins Ligation Co-Repressor Proteins 030217 neurology & neurosurgery HeLa Cells |
| Zdroj: | Science |
| ISSN: | 1095-9203 0036-8075 |
| DOI: | 10.1126/science.aaw5569 |
| Popis: | 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 |
| Databáze: | OpenAIRE |
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