Structure of a yeast catalytic step I spliceosome at 3.4 Å resolution

Author:

Wan Ruixue1,Yan Chuangye1,Bai Rui1,Huang Gaoxingyu1,Shi Yigong1

Affiliation:

1. Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.

Abstract

How spliceosomes make the first cut In eukaryotes, transcribed precursor mRNA includes noncoding sequences that must be spliced out. This is done by the spliceosome, a dynamic complex in which five small nuclear RNAs and several proteins go through a series of ordered interactions and conformational rearrangements to achieve splicing. Two protein structures provide a look at the first catalytic step in the pathway. Yan et al. report the structure of the activated spliceosome (the B act complex) at 3.5 Å resolution, revealing how latency is maintained even though the complex is mostly primed for catalysis. Wan et al. report the structure of the catalytic step 1 spliceosome (the C complex) at 3.4 Å resolution; this complex forms after the first step of the splicing reaction. Science , this issue pp. 904 and 895

Funder

Ministry of Science and Technology

National Natural Science Foundation of China

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference93 articles.

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