Postcatalytic spliceosome structure reveals mechanism of 3′–splice site selection

Author:

Wilkinson Max E.ORCID,Fica Sebastian M.,Galej Wojciech P.,Norman Christine M.,Newman Andrew J.,Nagai KiyoshiORCID

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

H2020 European Research Council

Medical Research Council

European Research Council

Cambridge Rutherford Memorial Scholarship

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Cited by 94 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3