Poly[ADP-ribose] polymerase in base excision repair: always engaged, but not essential for DNA damage processing

• Autorzy: Allinson S. L. , Dianova I.I. , Dianov G.L.
• Języki publikacji: EN

Abstrakty

EN

Poly(ADP-ribose) polymerase (PARP-1) is an abundant nuclear protein with a high affinity for single- and double-strand DNA breaks. Its binding to strand breaks pro­motes catalysis of the covalent modification of nuclear proteins with poly(ADP-ribose) synthesised from NAD+ . PARP-1-knockout cells are extremely sen­sitive to alkylating agents, suggesting the involvement of PARP-1 in base excision re­pair; however, its role remains unclear. We investigated the dependence of base exci­sion repair pathways on PARP-1 and NAD+ using whole cell extracts derived from normal and PARP-1 deficient mouse cells and DNA substrates containing abasic sites. In normal extracts the rate of repair was highly dependent on NAD+ . We found that in the absence of NAD+ repair was slowed down 4-6-fold after incision of the abasic site. We also established that in extracts from PARP-1 deficient mouse cells, repair of both regular and reduced abasic sites was increased with respect to normal extracts and was NAD+ -independent, suggesting that in both short- and long-patch BER PARP-1 slows down, rather than stimulates, the repair reaction. Our data support the pro­posal that PARP-1 does not play a major role in catalysis of DNA damage processing via either base excision repair pathway.

Słowa kluczowe

EN

poly[ADP-ribose] polymerase-1; cell extract; base excision repair; DNA repair; DNA damage; in vitro

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2003
• Tom: 50
• Numer: 1
• Opis fizyczny: p.169-179,fig.

Twórcy

autor

Allinson S. L.

• Medical Research Council, Harwell Oxfordshire, OX11 ORD, U.K.

autor

Dianova I.I.

autor

Dianov G.L.

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