 |
Journal articles
Brr2p carboxy-terminal Sec63 domain modulates Prp16 splicing RNA helicase.
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.
https://hal-pasteur.archives-ouvertes.fr/pasteur-01427502
Contributor : Anne Lassailly-Bondaz <>
Submitted on : Thursday, January 5, 2017 - 5:19:39 PM
Last modification on : Friday, April 10, 2020 - 5:26:24 PM
Long-term archiving on: : Thursday, April 6, 2017 - 2:35:19 PM
Contributor : Anne Lassailly-Bondaz <>
Submitted on : Thursday, January 5, 2017 - 5:19:39 PM
Last modification on : Friday, April 10, 2020 - 5:26:24 PM
Long-term archiving on: : Thursday, April 6, 2017 - 2:35:19 PM
File
gku1238.pdf
Publication funded by an institution
Licence
Distributed under a Creative Commons Attribution 4.0 International License