Publication: MRGBP, a member of the NuA4 complex, inhibits DNA double-strand break repair
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Identifiers
Date
2021-12-21
Authors
Rivero, Sabrina
Rodríguez-Real, Guillermo
Marín, Inés
Huertas, Pablo
Advisors
Journal Title
Journal ISSN
Volume Title
Publisher
John Wiley & Sons Ltd.
Abstract
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.
Description
MeSH Terms
Medical Subject Headings::Anatomy::Cells::Cells, Cultured::Cell Line::Cell Line, Tumor
Medical Subject Headings::Phenomena and Processes::Genetic Phenomena::Genetic Processes::DNA Damage::DNA Breaks::DNA Breaks, Double-Stranded
Medical Subject Headings::Phenomena and Processes::Genetic Phenomena::Genetic Processes::DNA Repair::DNA End-Joining Repair
Medical Subject Headings::Chemicals and Drugs::Enzymes and Coenzymes::Enzymes::Transferases::Acyltransferases::Acetyltransferases::Histone Acetyltransferases
Medical Subject Headings::Organisms::Eukaryota::Animals::Chordata::Vertebrates::Mammals::Primates::Haplorhini::Catarrhini::Hominidae::Humans
Medical Subject Headings::Chemicals and Drugs::Amino Acids, Peptides, and Proteins::Proteins::Nuclear Proteins
Medical Subject Headings::Phenomena and Processes::Genetic Phenomena::Genetic Processes::Recombination, Genetic::Homologous Recombination::Recombinational DNA Repair
Medical Subject Headings::Phenomena and Processes::Chemical Phenomena::Biochemical Phenomena::Biochemical Processes::DNA Repair
Medical Subject Headings::Phenomena and Processes::Chemical Phenomena::Biochemical Phenomena::Biochemical Processes::Down-Regulation
Medical Subject Headings::Phenomena and Processes::Genetic Phenomena::Genetic Processes::DNA Damage::DNA Breaks::DNA Breaks, Double-Stranded
Medical Subject Headings::Phenomena and Processes::Genetic Phenomena::Genetic Processes::DNA Repair::DNA End-Joining Repair
Medical Subject Headings::Chemicals and Drugs::Enzymes and Coenzymes::Enzymes::Transferases::Acyltransferases::Acetyltransferases::Histone Acetyltransferases
Medical Subject Headings::Organisms::Eukaryota::Animals::Chordata::Vertebrates::Mammals::Primates::Haplorhini::Catarrhini::Hominidae::Humans
Medical Subject Headings::Chemicals and Drugs::Amino Acids, Peptides, and Proteins::Proteins::Nuclear Proteins
Medical Subject Headings::Phenomena and Processes::Genetic Phenomena::Genetic Processes::Recombination, Genetic::Homologous Recombination::Recombinational DNA Repair
Medical Subject Headings::Phenomena and Processes::Chemical Phenomena::Biochemical Phenomena::Biochemical Processes::DNA Repair
Medical Subject Headings::Phenomena and Processes::Chemical Phenomena::Biochemical Phenomena::Biochemical Processes::Down-Regulation
DeCS Terms
CIE Terms
Keywords
DNA repair, DNA-end resection, MRGBP, TIP60, Recombination, Reparación del ADN, Lisina acetiltransferasa 5, Recombinación genética
Citation
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