- Tytuł:
- Poly(ADP-ribose) polymerase in base excision repair: always engaged, but not essential for DNA damage processing.
- Autorzy:
-
Allinson, Sarah
Dianova, Irina
Dianov, Grigory - Powiązania:
- https://bibliotekanauki.pl/articles/1043660.pdf
- Data publikacji:
- 2003
- Wydawca:
- Polskie Towarzystwo Biochemiczne
- Tematy:
-
PARP
base excision repair
cell extracts
in vitro repair
abasic sites
DNA repair - Opis:
- 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.
- Źródło:
-
Acta Biochimica Polonica; 2003, 50, 1; 169-179
0001-527X - Pojawia się w:
- Acta Biochimica Polonica
- Dostawca treści:
- Biblioteka Nauki
Artykuł