Werner syndrome protein prevents DNA breaks upon chromatin structure alteration
نویسندگان
چکیده
منابع مشابه
Werner syndrome protein interacts functionally with translesion DNA polymerases.
Werner syndrome (WS) is characterized by premature onset of age-associated disorders and predisposition to cancer. The WS protein, WRN, encodes 3' --> 5' DNA helicase and 3' --> 5' DNA exonuclease activities, and is implicated in the maintenance of genomic stability. Translesion (TLS) DNA polymerases (Pols) insert nucleotides opposite replication-blocking DNA lesions and presumably prevent repl...
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متن کاملIncreased chromosome instability and accumulation of DNA double-strand breaks in Werner syndrome cells.
Werner syndrome (WS) is a premature aging syndrome caused by mutations of the WRN gene. Here, we demonstrate that a strain of WS fibroblast cells shows abnormal karyotypes characterized by several complex translocations and 50-fold more frequency of abnormal metaphases including dicentric chromosomes without fragments than normal cells when examined at a similar culture stage. Further, telomere...
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DNA double-strand breaks (DSBs) can arise from multiple sources, including exposure to ionizing radiation. The repair of DSBs involves both posttranslational modification of nucleosomes and concentration of DNA-repair proteins at the site of damage. Consequently, nucleosome packing and chromatin architecture surrounding the DSB may limit the ability of the DNA-damage response to access and repa...
متن کاملAccumulation of Werner protein at DNA double-strand breaks in human cells.
Werner syndrome is an autosomal recessive accelerated-aging disorder caused by a defect in the WRN gene, which encodes a member of the RecQ family of DNA helicases with an exonuclease activity. In vitro experiments have suggested that WRN functions in several DNA repair processes, but the actual functions of WRN in living cells remain unknown. Here, we analyzed the kinetics of the intranuclear ...
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ژورنال
عنوان ژورنال: Aging Cell
سال: 2007
ISSN: 1474-9718,1474-9726
DOI: 10.1111/j.1474-9726.2007.00301.x