Brr2p carboxy-terminal Sec63 domain modulates Prp16 splicing RNA helicase |
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Authors: | Olivier Cordin Daniela Hahn Ross Alexander Amit Gautam Cosmin Saveanu J David Barrass Jean D Beggs |
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Institution: | 1.Wellcome Trust Centre for Cell Biology, University of Edinburgh, King''s Buildings, Mayfield Road, Edinburgh, EH9 3BF, UK;2.IBPC, CNRS FRE 3630, 13, rue Pierre & Marie Curie, 75005 Paris, France;3.Institut Pasteur, CNRS UMR3525, 25-28 rue du docteur Roux, 75015 Paris, France |
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Abstract: | RNA helicases are essential for virtually all cellular processes, however, their regulation is poorly understood. The activities of eight RNA helicases are required for pre-mRNA splicing. Amongst these, Brr2p is unusual in having two helicase modules, of which only the amino-terminal helicase domain appears to be catalytically active. Using genetic and biochemical approaches, we investigated interaction of the carboxy-terminal helicase module, in particular the carboxy-terminal Sec63-2 domain, with the splicing RNA helicase Prp16p. Combining mutations in BRR2 and PRP16 suppresses or enhances physical interaction and growth defects in an allele-specific manner, signifying functional interactions. Notably, we show that Brr2p Sec63-2 domain can modulate the ATPase activity of Prp16p in vitro by interfering with its ability to bind RNA. We therefore propose that the carboxy-terminal helicase module of Brr2p acquired a regulatory function that allows Brr2p to modulate the ATPase activity of Prp16p in the spliceosome by controlling access to its RNA substrate/cofactor. |
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