Mi-2/NuRD complex making inroads into DNA-damage response pathway.
In eukaryotic cells, packaging of DNA into highly condensed chromatin presents a significant obstacle to DNA-based processes. Cells use two major strategies including histone modifications and ATP-dependent chromatin remodeling to alter chromatin structure that allows protein factors to gain access to nucleosomal DNA. Beyond their well-established role in transcription, histone modifications and several classes of ATP-dependent chromatin-remodeling complex have been functionally linked to efficient DNA repair. Mi-2/nucleosome remodeling and histone deacetylation (NuRD) complex uniquely possess both nucleosome remodeling and histone deacetylation activities, which play a vital role in regulating transcription. However, the role of the Mi-2/NuRD complex in DNA damage response remains largely unexplored until now. Recent findings reveal that metastasis-associated protein 1 (MTA1), an integral component of the Mi-2/NuRD complex, has successfully made inroads into DNA damage response pathway, and thus, links two previously unconnected Mi-2/NuRD complex and DNA damage response research areas. In this review, we will summarize recent progress concerning the functions of histone modifications and chromatin remodeling in DNA repair, and discuss new role of Mi-2/NuRD complex in DNA damage response.
Li
Da-Qiang
DQ
Department of Biochemistry and Molecular Biology, George Washington University Medical Center, Washington, DC, USA.
Kumar
Rakesh
R
D000107:Acetylation; D000818:Animals; D004249:DNA Damage; D004260:DNA Repair; D006655:Histone Deacetylases / Q000235:genetics / Q000378:metabolism; D006657:Histones / Q000378:metabolism; D056245:Mi-2 Nucleosome Remodeling and Deacetylase Complex / Q000378:metabolism*; D051379:Mice; D012097:Repressor Proteins; D015534:Trans-Activators; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism
D006657:Histones; C503336:Mta1 protein, mouse; D012097:Repressor Proteins; D015534:Trans-Activators; D014157:Transcription Factors; D006655:Histone Deacetylases; D056245:Mi-2 Nucleosome Remodeling and Deacetylase Complex