Structural studies of the spliceosome: Bridging the gaps

被引:27
作者
Tholen, J. [1 ]
Galej, W. P. [1 ]
机构
[1] European Mol Biol Lab, 71 Ave Martyrs, F-38042 Grenoble, France
基金
欧洲研究理事会;
关键词
PRE-MESSENGER-RNA; CRYO-EM STRUCTURE; CRYSTAL-STRUCTURE; MINOR CLASS; U2; SNRNP; ATPASE; ARCHITECTURE; RECOGNITION; ACTIVATION; MUTATIONS;
D O I
10.1016/j.sbi.2022.102461
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The spliceosome is a multi-megadalton RNA-protein complex responsible for the removal of non-coding introns from pre-mRNAs. Due to its complexity and dynamic nature, it has proven to be a very challenging target for structural studies. Developments in single particle cr yo-EM have overcome these previous limitations and paved the way towards a structural characterisation of the splicing machinery. Despite tremendous progress, many aspects of spliceosome structure and function remain elusive. In particular, the events leading to the definition of exon-intron boundaries, alternative and non-canonical splicing events, and cross-talk with other cellular machineries. Efforts are being made to address these knowledge gaps and further our mechanistic understanding of the spliceosome. Here, we summarise recent progress in the structural and functional analysis of the spliceosome.
引用
收藏
页数:10
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