Structure of a human catalytic step I spliceosome

Splicing by the spliceosome involves branching and exon ligation. The branching reaction leads to the formation of the catalytic step I spliceosome (C complex). Here we report the cryo-electron microscopy structure of the human C complex at an average resolution of 4.1 angstroms. Compared with the C...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2018-02, Vol.359 (6375), p.537-545
Main Authors: Zhan, Xiechao, Yan, Chuangye, Zhang, Xiaofeng, Lei, Jianlin, Shi, Yigong
Format: Article
Language:English
Subjects:
Adenosine
Adenosine triphosphatase
Amino Acid Sequence
Biocatalysis
Catalysis
Catalytic Domain
Cryoelectron Microscopy
DEAD-box RNA Helicases - chemistry
DEAD-box RNA Helicases - ultrastructure
DNA helicase
Electron microscopy
Fungi
Humans
Microscopy
Models, Molecular
mRNA
Proteins
Ribonucleic acid
RNA
RNA Splicing
RNA Splicing Factors - chemistry
RNA Splicing Factors - ultrastructure
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - ultrastructure
Spliceosomes - chemistry
Spliceosomes - ultrastructure
Splicing
Splicing factors
Triphosphatase
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Summary:Splicing by the spliceosome involves branching and exon ligation. The branching reaction leads to the formation of the catalytic step I spliceosome (C complex). Here we report the cryo-electron microscopy structure of the human C complex at an average resolution of 4.1 angstroms. Compared with the C complex, the human complex contains 11 additional proteins. The step I splicing factors CCDC49 and CCDC94 (Cwc25 and Yju2 in , respectively) closely interact with the DEAH-family adenosine triphosphatase/helicase Prp16 and bridge the gap between Prp16 and the active-site RNA elements. These features, together with structural comparison of the human C and C* complexes, provide mechanistic insights into ribonucleoprotein remodeling and allow the proposition of a working mechanism for the C-to-C* transition.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.aar6401