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© Research
Publication : Nucleic acids research

Brr2p carboxy-terminal Sec63 domain modulates Prp16 splicing RNA helicase

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Nucleic acids research - 20 Jul 2015

Cordin O, Hahn D, Alexander R, Gautam A, Saveanu C, Barrass JD, Beggs JD

Link to Pubmed [PMID] – 25428373

Nucleic Acids Res. 2014 Dec;42(22):13897-910

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.

http://www.ncbi.nlm.nih.gov/pubmed/25428373