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• W2208526131 abstract "Upon DNA damage due to endogenous or exogenous causes, chromatin is dynamically modified, especially through posttranslational modifications (PTMs) of histones together with noncoding RNA expression. Both procedures modify accessibility of genes and regulatory genomic loci by protein factors and enzymes involved in gene expression as well as DNA repair processes. In addition, PTMs of proteins involved in genome integrity seem to play important roles in regulating their functions and protein–protein interactions (PPI). The most studied PTMs involved in DNA repair machinery function are histone phosphorylations, methylations/demethylations and to a lesser extent acetylations, allowing/prohibiting acces‐ sibility to double-strand break recognition and binding of factors/enzymes. Protein ubiquiti‐ nation – the covalent link of the small protein ubiquitin (Ub) to lysine residues of a target protein – was classically related to protein degradation, ensuring structural integrity control and/or protein turnover rate. This procedure involves the addition of multiple ubiquitin molecules in a specific manner, which targets the polyubiquitinated protein to the proteasome for degradation. In recent years, accumulating data unveiled a role for nondegrading ubiqui‐ tination of proteins involved in DNA repair pathways and cell fate decisions [1,2]. A welldocumented overview depicting the exceptional importance of ubiquitination in the restoration of genotoxic insults was carried out by a number of reviews, clearly pointing out ubiquitination and DNA damage response/repair interrelation [3]. The issue comprehensively covers practically all principal aspects of Ub function in the field. Therefore, many issues of the ubiquitin landscape at DNA double-strand breaks (DSBs) have been highlighted. As described, many challenges and puzzles remain to be solved regarding the intimate relation‐ ship between the DNA repair machinery and nondegrading ubiquitin signaling at DNA DSBs and the surrounding chromatin (Fig. 1) [3]." @default.
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• W2208526131 date "2015-11-18" @default.
• W2208526131 modified "2023-10-01" @default.
• W2208526131 title "Ubiquitination — An Evolving Role in DNA Repair" @default.
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• W2208526131 doi "https://doi.org/10.5772/61582" @default.
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