Download Chromatin dynamics in cellular function by Brehon Laurent PDF

By Brehon Laurent

This quantity contains well timed stories of numerous features of chromatin biology written through scientists on the vanguard of this quickly relocating box. subject matters lined comprise the constitution and serve as of protein modules inside of chromatin-remodeling proteins, newly characterised histone transformations (methylation, ubiquitylation) and their sensible results, transcription and histone dynamics, roles of chromatin home improvement components in DNA replication and service, and present types of nucleosome-remodeling mechanisms.

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Illustration of the known effector proteins of methylated histones shown above their cognate methyl lysine binding sites on the histone H3 and H4 tails. S. A. Grant created when H3 K9 was methylated in what is referred to as an “aromatic cage” (Fischle et al. 2003; Jacobs and Khorasanizadeh 2002). These studies support earlier findings that H3 K9Me targets the silencing protein, HP1, to heterochromatin (Bannister et al. 2001; Lachner et al. 2001; Nakayama et al. 2001). Interestingly, HP1 may form homodimers and subsequently compact chromatin into higher order heterochromatin structures when bound to histone H3 K9Me (Thiru et al.

Mol Cell 9(3):575–586 Mujtaba S et al. (2004) Structural mechanism of the bromodomain of the coactivator CBP in p53 transcriptional activation. Mol Cell 13(2):251–263 Nakayama J et al. (2001) Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly. Science 292(5514):110–113 Namboodiri VM et al. (2003) The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding. Structure (Camb) 11(2):175–186 Nameki N et al. (2005) Solution structure of the PWWP domain of the hepatoma-derived growth factor family.

2004) Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 119(7):941–953 Simic R et al. (2003) Chromatin remodeling protein Chd1 interacts with transcription elongation factors and localizes to transcribed genes. Embo J 22(8):1846–1856 Slater LM, Allen MD, Bycroft M (2003) Structural variation in PWWP domains. J Mol Biol 330(3):571–576 Smith TF et al. (1999) The WD repeat: a common architecture for diverse functions. Trends Biochem Sci 24(5):181–185 Stec I et al. (2000) The PWWP domain: a potential protein–protein interaction domain in nuclear proteins influencing differentiation?

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