English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

One, two, three: how histone methylation is read.

MPS-Authors
/persons/resource/persons15074

Fischle,  W.
Research Group of Chromatin Biochemistry, MPI for biophysical chemistry, Max Planck Society;

External Resource
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Fischle, W. (2012). One, two, three: how histone methylation is read. Epigenomics, 4(6), 641-653. doi:10.2217/epi.12.56.


Cite as: http://hdl.handle.net/11858/00-001M-0000-000E-7251-C
Abstract
Methylation of histone lysine and arginine residues constitutes a highly complex control system directing diverse functions of the genome. Owing to their immense signaling potential with distinct sites of methylation and defined methylation states of mono-, di- or trimethylation as well as their higher biochemical stability compared with other histone modifications, these marks are thought to be part of epigenetic regulatory networks. Biological principles of how histone methylation is read and translated have emerged over the last few years. Only very few methyl marks directly impact chromatin. Conversely, a large number of histone methylation binding proteins has been identified. These contain specialized modules that are recruited to chromatin in a methylation site- and state-specific manner. Besides the molecular mechanisms of interaction, patterns of regulation of the binding proteins are becoming evident.