Structure of a pre-catalytic spliceosome.
Structure of a pre-catalytic spliceosome.
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DOI:
10.1038/nature22799
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发表时间:
2017-06-29
期刊:
影响因子:
64.8
通讯作者:
Nagai K
中科院分区:
文献类型:
--
作者:
Plaschka C;Lin PC;Nagai K
Intron removal requires assembly of the spliceosome on pre-mRNA and extensive remodelling to form the spliceosome’s catalytic centre. Here we report the cryo-electron microscopy structure of the yeast pre-catalytic B complex spliceosome at near-atomic resolution. The mobile U2 snRNP associates with U4/U6.U5 tri-snRNP through U2/U6 helix II and an interface between U4/U6 di-snRNP and the U2 snRNP SF3b-containing domain, which also transiently contacts the helicase Brr2. The U2 snRNP 3’ region is flexibly attached to the SF3b-containing domain and protrudes over the concave surface of tri-snRNP, where the U1 snRNP may reside before its release from the pre-mRNA 5’-splice site. The U6 ACAGAGA sequence forms a hairpin which weakly tethers the 5’-splice site. B complex proteins Prp38, Snu23, and Spp381 bind the Prp8 N-terminal domain and stabilise U6 ACAGAGA stem–pre-mRNA and Brr2–U4 snRNA interactions. The results thus provide important insights into events leading to active site formation.
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