4.5 Article

CryoEM structures of two spliceosomal complexes: starter and dessert at the spliceosome feast

期刊

CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 36, 期 -, 页码 48-57

出版社

CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2015.12.005

关键词

-

资金

  1. Herchel Smith Research Studentship
  2. EMBO fellowship
  3. Medical Research Council [MC_U105184330]
  4. Medical Research Council [MC_U105184330] Funding Source: researchfish
  5. MRC [MC_U105184330] Funding Source: UKRI

向作者/读者索取更多资源

The spliceosome is formed on pre-mRNA substrates from five small nuclear ribonucleoprotein particles (U1, U2, U4/U6 and U5 snRNPs), and numerous non-snRNP factors. Saccharomyces cerevisiae U4/U6.U5 tri-snRNP comprises U5 snRNA, U4/U6 snRNA duplex and approximately 30 proteins and represents a substantial part of the spliceosome before activation. Schizosaccharomyces pombe U2.U6.U5 spliceosomal complex is a post-catalytic intron lariat spliceosome containing U2 and U5 snRNPs, NTC (nineteen complex), NTC-related proteins (NTR), U6 snRNA, and an RNA intron lariat. Two recent papers describe near-complete atomic structures of these complexes based on cryoEM single-particle analysis. The U4/U6.U5 tri-snRNP structure provides crucial insight into the activation mechanism of the spliceosome. The U2.U6.U5 complex reveals the striking architecture of NTC and NTR and important features of the group II intron-like catalytic RNA core remaining after spliced mRNA is released. These two structures greatly advance our understanding of the mechanism of pre-mRNA splicing.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.5
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据