Year: 2015
Type: article
Abstract: Although DNA double-strand break (DSB) repair is mediated by numerous proteins accumulated at DSB sites, how DNA repair proteins are assembled into damaged chromatin has not been fully elucidated. Here we show that a member of the tripartite motif protein family, TRIM29, is a histone-binding protein responsible for DNA damage response (DDR). We found that TRIM29 interacts with BRCA1-associated surveillance complex, cohesion, DNA-PKcs and components of TIP60 complex. The dynamics of the TRIM29-containing complex on H2AX nucleosomes is coordinated by a cross-talk between histone modifications. TRIM29 binds to modified histone H3 and H4 tails in the context of nucleosomes. Furthermore, chromatin binding of TRIM29 is required for the phosphorylation of H2AX and cell viability in response to ionizing radiation. Our results suggest that TRIM29 functions as a scaffold protein to assemble DNA repair proteins into chromatin followed by efficient activation of DDR. Many proteins are assembled into damaged chromatins to repair DNA double-strand breaks (DSBs). Here, the authors show that TRIM29 binds to modified histone H3 and H4 tails following DSB formation and functions as a scaffold protein to assemble DNA repair proteins into chromatin.
Source: Nature Communications
DOI: 10.1038/ncomms8299
Language: English
Topic: DNA Repair Mechanisms
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $6,990
Awards: Comprehensive analysis of TRIM type ubiquitin ligases in cell proliferation and differentiation, G1675169588, Biochemistry of Eukaryotic Messenger RNA Synthesis, G2158230864, G2515973659, Establishment of the strategy to purify transcription regulatory complex using immobilized DNA template, G4238086841, Regulation of signal transduction by TRIM family proteins, Analysis on the involvement of the new transcriptional elongation regulator Med26 in mixed acute leukemia
OpenAlex ID: W1668815300