Global S&T Development Trend Analysis Platform of Resources and Environment
DOI | 10.1002/joc.4694 |
Structure of a spliceosome remodelled for exon ligation | |
Fica, Sebastian M.1; Oubridge, Chris1; Galej, Wojciech P.1,2; Wilkinson, Max E.1; Bai, Xiao-Chen1; Newman, Andrew J.1; Nagai, Kiyoshi1 | |
2017-02-16 | |
发表期刊 | NATURE |
ISSN | 0028-0836 |
EISSN | 1476-4687 |
出版年 | 2017 |
卷号 | 542期号:7641页码:377-+ |
文章类型 | Article |
语种 | 英语 |
国家 | England; France |
英文摘要 | The spliceosome excises introns from pre-mRNAs in two sequential transesterifications-branching and exon ligation(1)-catalysed at a single catalytic metal site in U6 small nuclear RNA (snRNA)(2,3). Recently reported structures of the spliceosomal C complex(4,5) with the cleaved 5' exon and lariat-3'-exon bound to the catalytic centre revealed that branching-specific factors such as Cwc25 lock the branch helix into position for nucleophilic attack of the branch adenosine at the 5' splice site. Furthermore, the ATPase Prp16 is positioned to bind and translocate the intron downstream of the branch point to destabilize branching-specific factors and release the branch helix from the active site(4). Here we present, at 3.8 angstrom resolution, the cryo-electron microscopy structure of a Saccharomyces cerevisiae spliceosome stalled after Prp16-mediated remodelling but before exon ligation. While the U6 snRNA catalytic core remains firmly held in the active site cavity of Prp8 by proteins common to both steps, the branch helix has rotated by 75 degrees compared to the C complex and is stabilized in a new position by Prp17, Cef1 and the reoriented Prp8 RNase H-like domain. This rotation of the branch helix removes the branch adenosine from the catalytic core, creates a space for 3' exon docking, and restructures the pairing of the 5' splice site with the U6 snRNA ACAGAGA region. Slu7 and Prp18, which promote exon ligation, bind together to the Prp8 RNase H-like domain. The ATPase Prp22, bound to Prp8 in place of Prp16, could interact with the 3' exon, suggesting a possible basis for mRNA release after exon ligation(6,7). Together with the structure of the C complex(4), our structure of the C* complex reveals the two major conformations of the spliceosome during the catalytic stages of splicing. |
领域 | 地球科学 ; 气候变化 ; 资源环境 |
收录类别 | SCI-E |
WOS记录号 | WOS:000394451600043 |
WOS关键词 | PRE-MESSENGER-RNA ; CRYO-EM STRUCTURE ; ANGSTROM RESOLUTION ; SPLICING FACTOR ; ELECTRON CRYOMICROSCOPY ; FUNCTIONAL INTERACTIONS ; CRYSTAL-STRUCTURE ; CATALYTIC CENTER ; SITE CHOICE ; 2ND STEP |
WOS类目 | Multidisciplinary Sciences |
WOS研究方向 | Science & Technology - Other Topics |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://119.78.100.173/C666/handle/2XK7JSWQ/36701 |
专题 | 气候变化 |
作者单位 | 1.MRC, Mol Biol Lab, Francis Crick Ave, Cambridge CB2 0QH, England; 2.EMBL Grenoble, CS 90181, 71 Ave Martyrs, F-38042 Grenoble 9, France |
推荐引用方式 GB/T 7714 | Fica, Sebastian M.,Oubridge, Chris,Galej, Wojciech P.,et al. Structure of a spliceosome remodelled for exon ligation[J]. NATURE,2017,542(7641):377-+. |
APA | Fica, Sebastian M..,Oubridge, Chris.,Galej, Wojciech P..,Wilkinson, Max E..,Bai, Xiao-Chen.,...&Nagai, Kiyoshi.(2017).Structure of a spliceosome remodelled for exon ligation.NATURE,542(7641),377-+. |
MLA | Fica, Sebastian M.,et al."Structure of a spliceosome remodelled for exon ligation".NATURE 542.7641(2017):377-+. |
条目包含的文件 | 条目无相关文件。 |
除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。
修改评论