Document Detail


Novel regulatory principles of the spliceosomal Brr2 RNA helicase and links to retinal disease in humans.
MedLine Citation:
PMID:  24643059     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
For each round of pre-mRNA splicing, a spliceosome is assembled anew on its substrate. RNA-protein remodeling events required for spliceosome assembly, splicing catalysis, and spliceosome disassembly are driven and controlled by a conserved group of ATPases/RNA helicases. The activities of most of these enzymes are timed by their recruitment to the spliceosome. The Brr2 enzyme, however, which mediates spliceosome catalytic activation, is a stable subunit of the spliceosome, and thus, requires special regulation. Recent structural and functional studies have revealed diverse mechanisms whereby an RNaseH-like and a Jab1/MPN-like domain of the Prp8 protein regulate Brr2 activity during splicing both positively and negatively. Reversible Brr2 inhibition might in part be achieved via an intrinsically unstructured element of the Prp8 Jab1/MPN domain, a concept widespread in biological systems. Mutations leading to changes in the Prp8 Jab1/MPN domain, which are linked to a severe form of retinitis pigmentosa, disrupt Jab1/MPN-mediated regulation of Brr2.
Authors:
Sina Mozaffari-Jovin; Traudy Wandersleben; Karine F Santos; Cindy L Will; Reinhard Lührmann; Markus C Wahl
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2014-3-05
Journal Detail:
Title:  RNA biology     Volume:  11     ISSN:  1555-8584     ISO Abbreviation:  RNA Biol     Publication Date:  2014 Mar 
Date Detail:
Created Date:  2014-3-19     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101235328     Medline TA:  RNA Biol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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