Abstract:
:Group II intron RNAs self-splice in vitro but only at high salt and/or Mg2+ concentrations and have been thought to require proteins to stabilize their active structure for efficient splicing in vivo. Here, we show that a DEAD-box protein, CYT-19, can by itself promote the splicing and reverse splicing of the yeast aI5gamma and bI1 group II introns under near-physiological conditions by acting as an ATP-dependent RNA chaperone, whose continued presence is not required after RNA folding. Our results suggest that the folding of some group II introns may be limited by kinetic traps and that their active structures, once formed, do not require proteins or high Mg2+ concentrations for structural stabilization. Thus, during evolution, group II introns could have spliced and transposed by reverse splicing by using ubiquitous RNA chaperones before acquiring more specific protein partners to promote their splicing and mobility. More generally, our results provide additional evidence for the widespread role of RNA chaperones in folding cellular RNAs.
journal_name
Proc Natl Acad Sci U S Aauthors
Mohr S,Matsuura M,Perlman PS,Lambowitz AMdoi
10.1073/pnas.0600332103keywords:
subject
Has Abstractpub_date
2006-03-07 00:00:00pages
3569-74issue
10eissn
0027-8424issn
1091-6490pii
0600332103journal_volume
103pub_type
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