Length-dependent degradation of single-stranded 3' ends by the Werner syndrome protein (WRN): implications for spatial orientation and coordinated 3' to 5' movement of its ATPase/helicase and exonuclease domains.

TitleLength-dependent degradation of single-stranded 3' ends by the Werner syndrome protein (WRN): implications for spatial orientation and coordinated 3' to 5' movement of its ATPase/helicase and exonuclease domains.
Publication TypeJournal Article
Year of Publication2006
JournalBMC molecular biology
Volume7
Pagination6
Date Published2006 Feb 17
AbstractThe cancer-prone and accelerated aging disease Werner syndrome is caused by loss of function of the WRN gene product that possesses ATPase, 3' to 5' helicase and 3' to 5' exonuclease activities. Although WRN has been most prominently suggested to function in telomere maintenance, resolution of replication blockage and/or recombinational repair, its exact role in DNA metabolism remains unclear. WRN is the only human RecQ family member to possess both helicase and exonuclease activity, but the mechanistic relationship between these activities is unknown. In this study, model single-stranded and 3' overhang DNA substrates of varying length and structure were used to examine potential coordination between the ATPase/helicase and exonuclease activities of WRN.
URLhttps://bmcmolbiol.biomedcentral.com/articles/10.1186/1471-2199-7-6
DOI10.1186/1471-2199-7-6
PubMed Linkhttp://www.ncbi.nlm.nih.gov/pubmed/16503984?dopt=Abstract
Short TitleBMC Mol Biol