Brr2p carboxy-terminal Sec63 domain modulates Prp16 splicing RNA helicase

Oliver Cordin, Daniela Hahn, Ross Alexander, Amit Gautum, Cosmin Saveanu, J. David Barrass, Jean D. Beggs

Research output: Contribution to journalArticle

8 Citations (Scopus)
1 Downloads (Pure)

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.
Original languageEnglish
Pages (from-to)13897-13910
Number of pages14
JournalNucleic Acids Research
Volume42
Issue number22
DOIs
Publication statusPublished - 16 Dec 2014

Fingerprint Dive into the research topics of 'Brr2p carboxy-terminal Sec63 domain modulates Prp16 splicing RNA helicase'. Together they form a unique fingerprint.

  • Cite this

    Cordin, O., Hahn, D., Alexander, R., Gautum, A., Saveanu, C., Barrass, J. D., & Beggs, J. D. (2014). Brr2p carboxy-terminal Sec63 domain modulates Prp16 splicing RNA helicase. Nucleic Acids Research, 42(22), 13897-13910. https://doi.org/10.1093/nar/gku1238