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2014 ; 1839
(8
): 686-93
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Towards understanding methyllysine readout
#MMPMID24727128
Musselman CA
; Khorasanizadeh S
; Kutateladze TG
Biochim Biophys Acta
2014[Aug]; 1839
(8
): 686-93
PMID24727128
show ga
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
methyllysine-specific readers. MAJOR CONCLUSIONS: New studies reveal various
reader-nucleosome contacts outside the methylated histone tail, thus offering a
better model for association of histone readers to chromatin and broadening our
understanding of the functional implications of these interactions. In addition,
some progress has been made in the design of antagonists of these interactions.
GENERAL SIGNIFICANCE: Specific lysine methylation patterns are commonly
associated with certain chromatin states and genomic elements, and are linked to
distinct biological outcomes such as transcription activation or repression.
Disruption of patterns of histone modifications is associated with a number of
diseases, and there is tremendous therapeutic potential in targeting histone
modification pathways. Thus, investigating binding of readers of these
modifications is not only important for elucidating fundamental mechanisms of
chromatin regulation, but also necessary for the design of targeted therapeutics.
This article is part of a Special Issue entitled: Molecular mechanisms of histone
modification function.
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