Merck

Towards understanding methyllysine readout.

Biochimica et biophysica acta (2014-04-15)
Catherine A Musselman, Sepideh Khorasanizadeh, Tatiana G Kutateladze
ABSTRACT

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. 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. 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. 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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
L-Lysine acetate salt, ≥98% (HPLC)
Sigma-Aldrich
L-Lysine, crystallized, ≥98.0% (NT)
Supelco
L-Lysine, analytical standard
Sigma-Aldrich
L-Lysine, Vetec, reagent grade, ≥98%
Lysine acetate, European Pharmacopoeia (EP) Reference Standard
Sigma-Aldrich
L-Lysine, ≥98% (TLC)
Sigma-Aldrich
L-Lysine monohydrochloride, from non-animal source, meets EP, JP, USP testing specifications, suitable for cell culture, 98.5-101.0%
Sigma-Aldrich
L-Lysine monohydrochloride, reagent grade, ≥98% (HPLC)
Sigma-Aldrich
L-Lysine monohydrochloride, BioUltra, ≥99.5% (AT)
Supelco
L-Lysine monohydrochloride, Pharmaceutical Secondary Standard; Certified Reference Material
Supelco
L-Lysine monohydrochloride, certified reference material, TraceCERT®
Sigma-Aldrich
L-Lysine monohydrochloride, Vetec, reagent grade, ≥98%
Lysine hydrochloride, European Pharmacopoeia (EP) Reference Standard
Supelco
L-Lysine Acetate, Pharmaceutical Secondary Standard; Certified Reference Material