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Review
. 2011 Mar;21(3):381-95.
doi: 10.1038/cr.2011.22. Epub 2011 Feb 15.

Regulation of chromatin by histone modifications

Affiliations
Review

Regulation of chromatin by histone modifications

Andrew J Bannister et al. Cell Res. 2011 Mar.

Abstract

Chromatin is not an inert structure, but rather an instructive DNA scaffold that can respond to external cues to regulate the many uses of DNA. A principle component of chromatin that plays a key role in this regulation is the modification of histones. There is an ever-growing list of these modifications and the complexity of their action is only just beginning to be understood. However, it is clear that histone modifications play fundamental roles in most biological processes that are involved in the manipulation and expression of DNA. Here, we describe the known histone modifications, define where they are found genomically and discuss some of their functional consequences, concentrating mostly on transcription where the majority of characterisation has taken place.

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Figures

Figure 1
Figure 1
Domains binding modified histones. Examples of proteins with domains that specifically bind to modified histones as shown (updated from reference ).
Figure 2
Figure 2
Histone modification cross-talk. Histone modifications can positively or negatively affect other modifications. A positive effect is indicated by an arrowhead and a negative effect is indicated by a flat head (updated from reference ).
Figure 3
Figure 3
Interplay of factors at an active gene in yeast (adapted from references and ).

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References

    1. Allfrey VG, Faulkner R, Mirsky AE. Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc Natl Acad Sci USA. 1964;51:786–794. - PMC - PubMed
    1. Luger K, Mader AW, Richmond RK, Sargent DF, Richmond TJ. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature. 1997;389:251–260. - PubMed
    1. Xhemalce B, Dawson MA, Bannister AJ.Histone modificationsIn: Meyers R, ed. Encyclopedia of Molecular Cell Biology and Molecular Medicine. John Wiley and Sons; 2011. In Press.
    1. Parthun MR. Hat1: the emerging cellular roles of a type B histone acetyltransferase. Oncogene. 2007;26:5319–5328. - PubMed
    1. Hodawadekar SC, Marmorstein R. Chemistry of acetyl transfer by histone modifying enzymes: structure, mechanism and implications for effector design. Oncogene. 2007;26:5528–5540. - PubMed

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