Structure of the yeast spliceosomal postcatalytic P complex-Reference-Cited by-同舟云学术

Structure of the yeast spliceosomal postcatalytic P complex

Published:2017-12-08 Issue:6368 Volume:358 Page:1278-1283
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Liu Shiheng¹²^ORCID,Li Xueni³^ORCID,Zhang Lingdi³^ORCID,Jiang Jiansen¹²,Hill Ryan C.³^ORCID,Cui Yanxiang¹^ORCID,Hansen Kirk C.³^ORCID,Zhou Z. Hong¹²^ORCID,Zhao Rui³^ORCID

Affiliation:

1. Electron Imaging Center for Nanomachines, University of California, Los Angeles (UCLA), Los Angeles, CA 90095, USA.

2. Department of Microbiology, Immunology, and Molecular Genetics, UCLA, Los Angeles, CA 90095, USA.

3. Department of Biochemistry and Molecular Genetics, University of Colorado Denver (UCD), Anschutz Medical Campus, Aurora, CO 80045, USA.

Abstract

Understanding splicing from the 3′ end The spliceosome removes introns from eukaryotic mRNA precursors and yields mature transcripts by joining exons. Despite decades of functional studies and recent progress in understanding the spliceosome structure, the mechanism by which the 3′ splice site (SS) is recognized by the spliceosome has remained unclear. Liu et al. and Wilkinson et al. report the high-resolution cryo-electron microscopy structures of the yeast postcatalytic spliceosome. The structures reveal that the 3′SS is recognized through non-Watson-Crick base pairing with the 5′SS and the branch point, stabilized by the intron region and protein factors. Science , this issue p. 1278 , p. 1283

Funder

NIH Office of the Director

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference54 articles.

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4. Cryo-EM structure of the spliceosome immediately after branching

5. Structure of a yeast step II catalytically activated spliceosome

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