A helical bundle in the N-terminal domain of the BLM helicase mediates dimer and potentially hexamer formation.

ABSTRACT: Helicases play a critical role in processes such as replication or recombination by unwinding double-stranded DNA; mutations of these genes can therefore have devastating biological consequences. In humans, mutations in genes of three members of the RecQ family helicases (blm, wrn, and recq4) give rise to three strikingly distinctive clinical phenotypes: Bloom syndrome, Werner syndrome, and Rothmund-Thomson syndrome, respectively. However, the molecular basis for these varying phenotypic outcomes is unclear, in part because a full mechanistic description of helicase activity is lacking. Because the helicase core domains are highly conserved, it has been postulated that functional differences among family members might be explained by significant differences in the N-te

SUBMITTER: Shi J 

PROVIDER: S-EPMC5392582 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature