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However, loading of acetylated H3K56 may occur earlier and function to hold the chromatin in an open structure to help in the repair process. Determination of the timing of H3K56 acetylation in human cells at the sites of damage will help settle this matter. Similarly, elucidating the kinetics of deacetylation at this residue following repair will clarify whether this H3K56ac needs to be removed to restore chromatin to its original/unmodified state for the full repair process to be completed. The Modification of Linker Histones During DNA Repair The linker histone, H1, associates with the inter-nucleosomal linker DNA.
Nature, 453, 682–686. Botuyan, M. , Ward, I. , Kim, J. , Thompson, J. , and Mer, G. (2006) Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair. Cell, 127, 1361–1373. Botuyan, M. , and Mer, G. (2004) Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains. Structure, 12, 1137–1146. Bradbury, E. M. (1992) Reversible histone modifications and the chromosome cell cycle. Bioessays, 14, 9–16. Bryan, E. , Jokubaitis, V.
This pathway involves enzymes that ubiquitylate the histones H2A, H2B and H2AX at sites of DNA damage, subsequent recruitment of factors that recognize and bind to these modified histones, and co-recruitement of important DDR proteins such as BRCA1. , 2007). RNF8 accumulates at sites of damage shortly after recruitment of γH2AX, MDC1 and NBS1. , 2007). E. Chubb and S. , 2007). Another E3 ligase, RNF168 (RING finger protein 168), also accumulates at damage sites in an RNF8-dependent manner. In addition to its RING finger domain, RNF168 contains two MIU (motif interacting with ubiquitin) domains, which it uses to bind to histones ubiquitylated by RNF8.