The Werner syndrome helicase and exonuclease cooperate to resolve telomeric D loops in a manner regulated by TRF1 and TRF2.
作者： Patricia L Opresko , Marit Otterlei , Jesper Graakjær , Per Bruheim , Lale Dawut
DOI: 10.1016/J.MOLCEL.2004.05.023
关键词:
摘要: Werner syndrome (WS) is characterized by features of premature aging and caused loss the RecQ helicase protein WRN. WS fibroblasts display defects associated with telomere dysfunction, including accelerated erosion senescence. In yeast, helicases act in an alternative pathway for lengthening (ALT) via homologous recombination. We found that WRN associates telomeres when dissociation telomeric D loops likely during replication human ALT cells, directly DNA. The majority TRF1/PCNA colocalizing foci contained live S phase cells but not telomerase-positive HeLa cells. Biochemically, 3' to 5' exonuclease simultaneously cooperate release invading tail from a loop vitro. binding proteins TRF1 TRF2 limit digestion propose roles dissociating structures telomerase-deficient
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