RT Journal Article
T1 MRGBP, a member of the NuA4 complex, inhibits DNA double-strand break repair
A1 Rivero, Sabrina
A1 Rodríguez-Real, Guillermo
A1 Marín, Inés
A1 Huertas, Pablo
K1 DNA repair
K1 DNA-end resection
K1 MRGBP
K1 TIP60
K1 Recombination
K1 Reparación del ADN
K1 Lisina acetiltransferasa 5
K1 Recombinación genética
AB The repair of DNA breaks takes place in the context of chromatin and thus involves the activity of chromatin remodelers. The nucleosome acetyltransferase of H4 (NuA4) remodeler complex enables DNA break repair by relaxing flanking chromatin. Here, we show that MRG domain binding protein (MRGBP), a member of this complex, acts as a general inhibitor of DNA double-strand break repair. Upon its downregulation, repair is generally increased. This is particularly evident for the stimulation of early events of homologous recombination. Thus, MRGBP has an opposing role to the main catalytic subunits of the NuA4 complex. Our data suggest that MRGBP acts by limiting the activity of this complex in DNA repair, specifically by narrowing the extent of DNA-end resection.
PB John Wiley & Sons Ltd.
YR 2021
FD 2021-12-21
LK http://hdl.handle.net/10668/3549
UL http://hdl.handle.net/10668/3549
LA en
NO Rivero S, Rodríguez-Real G, Marín I, Huertas P. MRGBP, a member of the NuA4 complex, inhibits DNA double-strand break repair. FEBS Open Bio. 2021 11: 622-632
DS RISalud
RD Apr 7, 2025