ArticleAge (Dordrecht, Netherlands)2013
The Drosophila orthologue of progeroid human WRN exonuclease, DmWRNexo, cleaves replication substrates but is inhibited by uracil or abasic sites : analysis of DmWRNexo activity in vitro.
Article in Age (Dordrecht, Netherlands), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Werner syndrome exonuclease promotes gut regeneration and causes age-associated gut hyperplasia in Drosophila.PLoS biology · 2025Article
- Dietary restriction fails to extend lifespan of Drosophila model of Werner syndrome.G3 (Bethesda, Md.) · 2024Article
- Characterization of Stress Responses in aBiomolecules · 2021Article
- Evidence for premature aging in a Drosophila model of Werner syndrome.Experimental gerontology · 2019Article
- Lifespan and Stress Resistance in Drosophila with Overexpressed DNA Repair Genes.Scientific reports · 2015Article
- The Drosophila Werner exonuclease participates in an exonuclease-independent response to replication stress.Genetics · 2014Article
- A fluorescence-based exonuclease assay to characterize DmWRNexo, orthologue of human progeroid WRN exonuclease, and its application to other nucleases.Journal of visualized experiments : JoVE · 2013Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Werner syndrome (WS) is a rare late-onset premature ageing disease showing many of the phenotypes associated with normal ageing, and provides one of the best models for investigating cellular pathways that lead to normal ageing. WS is caused by mutation of WRN, which encodes a multifunctional DNA replication and repair helicase/exonuclease. To investigate the role of WRN protein's unique exonuclease domain, we have recently identified DmWRNexo, the fly orthologue of the exonuclease domain of human WRN. Here, we fully characterise DmWRNexo exonuclease activity in vitro, confirming 3'-5' polarity, demonstrating a requirement for Mg(2+), inhibition by ATP, and an ability to degrade both single-stranded DNA and duplex DNA substrates with 3' or 5' overhangs, or bubble structures, but with no activity on blunt ended DNA duplexes. We report a novel active site mutation that ablates enzyme activity. Lesional substrates containing uracil are partially cleaved by DmWRNexo, but the enzyme pauses on such substrates and is inhibited by abasic sites. These strong biochemical similarities to human WRN suggest that Drosophila can provide a valuable experimental system for analysing the importance of WRN exonuclease in cell and organismal ageing.
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