Nucleolin inhibits G4 oligonucleotide unwinding by Werner helicase.

ABSTRACT:

Background

The Werner protein (WRNp), a member of the RecQ helicase family, is strongly associated with the nucleolus, as is nucleolin (NCL), an important nucleolar constituent protein. Both WRNp and NCL respond to the effects of DNA damaging agents. Therefore, we have investigated if these nuclear proteins interact and if this interaction has a possible functional significance in DNA damage repair.

Methodology/principal findings

Here we report that WRNp interacts with the RNA-binding protein, NCL, based on immunoprecipitation, immunofluorescent co-localization in live and fixed cells, and direct binding of purified WRNp to nucleolin. We also map the binding region to the C-terminal domains of both proteins. Furthermore, treatment of U2OS cells with 15 µM of the Topoisomeras

SUBMITTER: Indig FE 

PROVIDER: S-EPMC3366963 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature