The diverse functions of histone lysine methylation

  title={The diverse functions of histone lysine methylation},
  author={Cyrus Martin and Yi Zhang},
  journal={Nature Reviews Molecular Cell Biology},
  • Cyrus Martin, Yi Zhang
  • Published 1 November 2005
  • Biology, Chemistry
  • Nature Reviews Molecular Cell Biology
Covalent modifications of histone tails have fundamental roles in chromatin structure and function. One such modification, lysine methylation, has important functions in many biological processes that include heterochromatin formation, X-chromosome inactivation and transcriptional regulation. Here, we summarize recent advances in our understanding of how lysine methylation functions in these diverse biological processes, and raise questions that need to be addressed in the future. 
Histone lysine methylation: an epigenetic modification?
Recent advances in the understanding of three intensely-studied histone lysine methylation marks are examined, focusing on the potential mechanisms by which these marks may be maintained during cell proliferation and adhere to the principles of epigenetics.
Histone lysine methylation in the context of nuclear architecture
The 3D architecture and spatial interrealtionships of different histone lysine methylation sites was investigated in various human cell types in a bid to understand the role of methylation in gene regulation.
Dynamic protein methylation in chromatin biology
This work examines how dynamic histone methylation contributes to normal cellular function in mammals and focuses on the recent advances in the understanding of the hist one methylation system.
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Recent advances in histone methyltransferases and histone demethylases are summarized in a review of recent advances in these mechanisms.
Is histone loss a common feature of DNA metabolism regulation?
  • A. Morillon
  • Biology
    Biochemistry and cell biology = Biochimie et biologie cellulaire
  • 2006
This review focuses on recently published work that describes the relationships between histone modification/exchange and nucleosome displacement.
Regulation of histone methylation by demethylimination and demethylation
The enzymatic and structural basis for the mechanisms that these enzymes use to counteract histone methylation are examined and insights into their substrate specificity and biological function are provided.
Histone lysine demethylases in Drosophila melanogaster
The current findings of the 13 known histone lysine demethylases in Drosophila melanogaster are summarized, and the critical role of these histone-modifying enzymes in the maintenance of genomic functions are discussed.


The language of covalent histone modifications
It is proposed that distinct histone modifications, on one or more tails, act sequentially or in combination to form a ‘histone code’ that is, read by other proteins to bring about distinct downstream events.
An epigenetic road map for histone lysine methylation
Histone N-termini (tails) undergo diverse post-translational modifications, including acetylation, phosphorylation, methylation, ubiquitination and ADP-ribosylation ([van Holde, 1988][1]; [Wolffe,
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The discovery of enzymes that reverse the methylation of lysines and arginines challenges current thinking on the unique nature of histone methylation, and substantially increases the complexity of hist one modification pathways.
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This work aims to demonstrate the efforts towards in-situ applicability of EMMARM, which aims to provide real-time information about the “building blocks” of EMT and its role in cancer progression.
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A genome-wide chromatin structure analysis in a higher eukaryote found a binary pattern of histone modifications among euchromatic genes, with active genes being hyperacetylated for H3 and H4 and hypermethylated at Lys 4 and Lys 79 of H3, and inactive genes being hypomethylated and deacetylation at the same residues.
Role of Histone H3 Lysine 9 Methylation in Epigenetic Control of Heterochromatin Assembly
In vivo evidence is provided that lysine 9 of histone H3 (H3 Lys9) is preferentially methylated by the Clr4 protein at heterochromatin-associated regions in fission yeast, defining a conserved pathway wherein sequential histone modifications establish a “histone code” essential for the epigenetic inheritance of heterochROMatin assembly.
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It is proposed that this epigenetic marking system represents a fundamental regulatory mechanism that has an impact on most, if not all, chromatin-templated processes, with far-reaching consequences for cell fate decisions and both normal and pathological development.
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A functional interdependence of site-specific H3 tail modifications is revealed and a dynamic mechanism for the regulation of higher-order chromatin is suggested.
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It is concluded that Set1 facilitates transcription, in part, by protecting active coding regions from deacetylation, in the context of recent studies showing that Lys 4 methylation precludes histone de acetylase recruitment.