Winged helix domains with unknown function in Hel308 and related helicases. (19th January 2011)

• Record Type: Journal Article
• Authors: Woodman, Isabel L.; Bolt, Edward L.
• Is Part Of: Biochemical Society transactions. Volume 39:Number 1(2011)
• Page Start: 140
• Page End: 144
• Publication Date: 2011-01-19
• Subjects: Brr2 -- DNA repair -- Hel308 -- Mtr4 -- Prp43p; Biochemistry -- Congresses; 572
• DOI: 10.1042/BST0390140
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : Hel308 is a superfamily 2 helicase/translocase that is conserved throughout archaea and in some eukaryotes for repair of genotoxic lesions such as ICLs (interstrand DNA cross-links). Atomic structures of archaeal Hel308 have allowed mechanistic insights into ATPase and helicase functions, but have also highlighted structures that currently lack a known function, such as an unexpected WH (winged helix) domain. This domain and similar overall protein structural organization was also identified in other superfamily 2 helicases that process RNA molecules in eukaryotes: Brr2, Mtr4 and Prp43p. We survey the structure of Hel308 with regard to its WH domain in particular and its function(s) in maintaining structural integrity of the overall Hel308 ring structure, and possibly during interactions of Hel308 with other proteins and/or forked DNA.