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Int. J. Mol. Sci. 2012, 13(10), 12461-12486; doi:10.3390/ijms131012461
Review

Implication of Posttranslational Histone Modifications in Nucleotide Excision Repair

Received: 21 August 2012; in revised form: 17 September 2012 / Accepted: 20 September 2012 / Published: 28 September 2012
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Abstract: Histones are highly alkaline proteins that package and order the DNA into chromatin in eukaryotic cells. Nucleotide excision repair (NER) is a conserved multistep reaction that removes a wide range of generally bulky and/or helix-distorting DNA lesions. Although the core biochemical mechanism of NER is relatively well known, how cells detect and repair lesions in diverse chromatin environments is still under intensive research. As with all DNA-related processes, the NER machinery must deal with the presence of organized chromatin and the physical obstacles it presents. A huge catalogue of posttranslational histone modifications has been documented. Although a comprehensive understanding of most of these modifications is still lacking, they are believed to be important regulatory elements for many biological processes, including DNA replication and repair, transcription and cell cycle control. Some of these modifications, including acetylation, methylation, phosphorylation and ubiquitination on the four core histones (H2A, H2B, H3 and H4) or the histone H2A variant H2AX, have been found to be implicated in different stages of the NER process. This review will summarize our recent understanding in this area.
Keywords: nucleotide excision repair; global genomic repair; histone modifications; acetylation; methylation; phosphorylation; ubiquitination nucleotide excision repair; global genomic repair; histone modifications; acetylation; methylation; phosphorylation; ubiquitination
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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MDPI and ACS Style

Li, S. Implication of Posttranslational Histone Modifications in Nucleotide Excision Repair. Int. J. Mol. Sci. 2012, 13, 12461-12486.

AMA Style

Li S. Implication of Posttranslational Histone Modifications in Nucleotide Excision Repair. International Journal of Molecular Sciences. 2012; 13(10):12461-12486.

Chicago/Turabian Style

Li, Shisheng. 2012. "Implication of Posttranslational Histone Modifications in Nucleotide Excision Repair." Int. J. Mol. Sci. 13, no. 10: 12461-12486.


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