Structural studies of the spliceosome: zooming into the heart of the machine.
Structural studies of the spliceosome: zooming into the heart of the machine.
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DOI:
10.1016/j.sbi.2013.12.002
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发表时间:
2014-04
影响因子:
6.8
通讯作者:
Nagai K
中科院分区:
文献类型:
--
作者:
Galej WP;Nguyen TH;Newman AJ;Nagai K
Structures of Prp8 and Brr2 have been determined. Insights into the active site cavity of the spliceosome. New evolutionary links between spliceosomes and group II introns. Ligands of the catalytic magnesium ions have been found. Spliceosomes are large, dynamic ribonucleoprotein complexes that catalyse the removal of introns from messenger RNA precursors via a two-step splicing reaction. The recent crystal structure of Prp8 has revealed Reverse Transcriptase-like, Linker and Endonuclease-like domains. The intron branch-point cross-link with the Linker domain of Prp8 in active spliceosomes and together with suppressors of 5′ and 3′ splice site mutations this unambiguously locates the active site cavity. Structural and mechanistic similarities with group II self-splicing introns have encouraged the notion that the spliceosome is at heart a ribozyme, and recently the ligands for two catalytic magnesium ions were identified within U6 snRNA. They position catalytic divalent metal ions in the same way as Domain V of group II intron RNA, suggesting that the spliceosome and group II intron use the same catalytic mechanisms.
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