The splicing of yeast mitochondrial group I and group II introns requires a DEAD-box protein with RNA chaperone function
The splicing of yeast mitochondrial group I and group II introns requires a DEAD-box protein with RNA chaperone function
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DOI:
10.1073/pnas.0407896101
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发表时间:
2005-01-04
影响因子:
11.1
通讯作者:
Perlman, PS
中科院分区:
文献类型:
--
作者:
Huang, HR;Rowe, CE;Perlman, PS
Group I and II introns self-splice in vitro, but require proteins for efficient splicing in vivo, to stabilize the catalytically active RNA structure. Recent studies showed that the splicing of some Neurospora crassa mitochondrial group I introns additionally requires a DEAD-box protein, CYT-19, which acts as an RNA chaperone to resolve normative structures formed during RNA folding. Here we show that, in Saccharomyces cerevisiae mitochondria, a related DEAD-box protein, Mss116p, is required for the efficient splicing of all group I and II introns, some RNA end-processing reactions, and translation of a subset of mRNAs, and that all these defects can be partially or completely suppressed by the expression of CYT-19. Results for the al2 group II intron indicate that Mss116p is needed after binding the intron-encoded maturase, likely for the disruption of stable but inactive RNA structures. Our results suggest that both group I and II introns are prone to kinetic traps in RNA folding in vivo and that the splicing of both types of introns may require DEAD-box proteins that function as RNA chaperones.