Brr2p RNA helicase with a split personality: insights into structure and function. (26th July 2010)

• Record Type: Journal Article
• Authors: Hahn, Daniela; Beggs, Jean D.
• Is Part Of: Biochemical Society transactions. Volume 38:Number 4(2010)
• Page Start: 1105
• Page End: 1109
• Publication Date: 2010-07-26
• Subjects: Brr2 protein -- pre-mRNA processing factor 8 (PRP8) -- retinitis pigmentosa (RP) -- splicing -- tri-small nuclear ribonucleoprotein (tri-snRNP) -- U4/U6 small nuclear ribonucleoprotein; Biochemistry -- Congresses; 572
• DOI: 10.1042/BST0381105
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : RNA helicases are involved in many cellular processes. Pre-mRNA splicing requires eight different DExD/H-box RNA helicases, which facilitate spliceosome assembly and remodelling of the intricate network of RNA rearrangements that are central to the splicing process. Brr2p, one of the spliceosomal RNA helicases, stands out through its unusual domain architecture. In the present review we highlight the advances made by recent structural and biochemical studies that have important implications for the mechanism and regulation of Brr2p activity. We also discuss the involvement of human Brr2 in retinitis pigmentosa, a degenerative eye disease, and how its functions in splicing might connect to the molecular pathology of the disease.