Common Design Principles in the Spliceosomal RNA Helicase Brr2 and in the Hel308 DNA Helicase

Abstract

(Molecular Cell 35, 454–466; August 28, 2009) In our study of the spliceosomal Brr2 helicase, we incorrectly labeled a fragment of the protein Prp8 that we used in activity assays of Brr2 and Brr2 mutants. Throughout the main text and Supplemental Information, we inadvertently referred to the fragment as “Prp8(1796-2092)”; however, the correct fragment we used is “Prp8(1806-2413)”. We apologize for any inconvenience this may have caused. Common Design Principles in the Spliceosomal RNA Helicase Brr2 and in the Hel308 DNA HelicasePena et al.Molecular CellAugust 28, 2009In BriefBrr2 is a unique DExD/H box protein required for catalytic activation and disassembly of the spliceosome. It contains two tandem helicase cassettes that both comprise dual RecA-like domains and a noncanonical Sec63 unit. The latter may bestow the enzyme with unique properties. We have determined crystal structures of the C-terminal Sec63 unit of yeast Brr2, revealing three domains, two of which resemble functional modules of a DNA helicase, Hel308, despite lacking significant sequence similarity. Full-Text PDF Open Archive