Histone modifications during DNA replication
Faithful and accurate replication of the DNA molecule is essential for eukaryote organisms. Nonetheless, in the last few years it has become evident that inheritance of the chromatin states associated with different regions of the genome is as important as the faithful inheritance of the DNA sequence itself. Such chromatin states are determined by a multitude of factors that act to modify not only the DNA molecule, but also the histone proteins associated with it. For instance, histones can be posttranslationally modified, and it is well established that these posttranslational marks are involved in several essential nuclear processes such as transcription and DNA repair. However, recent evidence indicates that posttranslational modifications of histones might be relevant during DNA replication. Hence, the aim of this review is to describe the most recent publications related to the role of histone posttranslational modifications during DNA replication.
Keywordsacetylation chromatin remodeling DNA replication histone methylation phosphorylation post translational modification ubiquitination
Unable to display preview. Download preview PDF.
- Barman, H.K., Takami, Y., Ono, T., Nishijima, H., Sanematsu, F., Shibahara, K., and Nakayama, T. (2006). Histone acetyltransferase 1 is dispensable for replication-coupled chromatin assembly but contributes to recover DNA damages created following replication blockage in vertebrate cells. Biochem. Biophys. Res. Commun. 345, 1547–1557.PubMedCrossRefGoogle Scholar
- Collins, S.R., Miller, K.M., Maas, N.L., Roguev, A., Fillingham, J., Chu, C.S., Schuldiner, M., Gebbia, M., Recht, J., Shales, M., et al. (2007). Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map. Nature 446, 806–810.PubMedCrossRefGoogle Scholar
- Deterding, L.J., Bunger, M.K., Banks, G.C., Tomer, K.B., and Archer, T.K. (2008). Global changes in and characterization of specific sites of phosphorylation in mouse and human histone H1 Isoforms upon CDK inhibitor treatment using mass spectrometry. J. Proteome Res. 7, 2368–2379.PubMedCrossRefGoogle Scholar
- Fan, Y., Nikitina, T., Zhao, J., Fleury, T.J., Bhattacharyya, R., Bouhassira, E.E., Stein, A., Woodcock, C.L., and Skoultchi, A.I. (2005). Histone H1 depletion in mammals alters global chromatin structure but causes specific changes in gene regulation. Cell 123, 1199–1212.PubMedCrossRefGoogle Scholar
- Fang, J., Feng, Q., Ketel, C.S., Wang, H., Cao, R., Xia, L., Erdjument-Bromage, H., Tempst, P., Simon, J.A., and Zhang, Y. (2002). Purification and functional characterization of SET8, a nucleosomal histone H4-lysine 20-specific methyltransferase. Curr. Biol. 12, 1086–1099.PubMedCrossRefGoogle Scholar
- Recht, J., Tsubota, T., Tanny, J.C., Diaz, R.L., Berger, J.M., Zhang, X., Garcia, B.A., Shabanowitz, J., Burlingame, A.L., Hunt, D.F., et al. (2006). Histone chaperone Asf1 is required for histone H3 lysine 56 acetylation, a modification associated with S phase in mitosis and meiosis. Proc. Natl. Acad. Sci. USA 103, 6988–6993.PubMedCrossRefGoogle Scholar