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Towards understanding methyllysine readout.


ABSTRACT:

Background

Lysine methylation is the most versatile covalent posttranslational modification (PTM) found in histones and non-histone proteins. Over the past decade a number of methyllysine-specific readers have been discovered and their interactions with histone tails have been structurally and biochemically characterized. More recently innovative experimental approaches have emerged that allow for studying reader interactions in the context of the full nucleosome and nucleosomal arrays.

Scope of review

In this review we give a brief overview of the known mechanisms of histone lysine methylation readout, summarize progress recently made in exploring interactions with methylated nucleosomes, and discuss the latest advances in the development of small molecule inhibitors of the

SUBMITTER: Musselman CA 

PROVIDER: S-EPMC4453862 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature

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