Investigation of the core binding regions of human Werner syndrome and Fanconi anemia group J helicases on replication protein A.

ABSTRACT: Werner syndrome protein (WRN) and Fanconi anemia group J protein (FANCJ) are human DNA helicases that contribute to genome maintenance. They interact with replication protein A (RPA), and these interactions dramatically enhance the unwinding activities of both helicases. Even though the interplay between these helicases and RPA is particularly important in the chemoresistance pathway of cancer cells, the precise binding regions, interfaces, and properties have not yet been characterized. Here we present systematic NMR analyses and fluorescence polarization anisotropy assays of both helicase-RPA interactions for defining core binding regions and binding affinities. Our results showed that two acidic repeats of human WRN bind to RPA70N and RPA70A. For FANCJ, the acidic-rich sequence in the C

SUBMITTER: Yeom G 

PROVIDER: S-EPMC6768877 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature