Molecular cooperation between the Werner syndrome protein and replication protein A in relation to replication fork blockage.

ABSTRACT: The premature aging and cancer-prone disease Werner syndrome is caused by loss of function of the RecQ helicase family member Werner syndrome protein (WRN). At the cellular level, loss of WRN results in replication abnormalities and chromosomal aberrations, indicating that WRN plays a role in maintenance of genome stability. Consistent with this notion, WRN possesses annealing, exonuclease, and ATPase-dependent helicase activity on DNA substrates, with particularly high affinity for and activity on replication and recombination structures. After certain DNA-damaging treatments, WRN is recruited to sites of blocked replication and co-localizes with the human single-stranded DNA-binding protein replication protein A (RPA). In this study we examined the physical and functional interaction bet

SUBMITTER: Machwe A 

PROVIDER: S-EPMC3030355 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature