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Molecular basis for substrate recognition by lysine methyltransferases and demethylases.

Biochimica et biophysica acta (2014-06-21)
Paul A Del Rizzo, Raymond C Trievel
ABSTRACT

Lysine methylation has emerged as a prominent covalent modification in histones and non-histone proteins. This modification has been implicated in numerous genomic processes, including heterochromatinization, cell cycle progression, DNA damage response, DNA replication, genome stability, and epigenetic gene regulation that underpins developmental programs defining cell identity and fate. The site and degree of lysine methylation is dynamically modulated through the enzymatic activities of protein lysine methyltransferases (KMTs) and protein lysine demethylases (KDMs). These enzymes display distinct substrate specificities that in part define their biological functions. This review explores recent progress in elucidating the molecular basis of these specificities, highlighting structural and functional studies of the methyltransferases SUV4-20H1 (KMT5B), SUV4-20H2 (KMT5C), and ATXR5, and the demethylases UTX (KDM6A), JMJD3 (KDM6B), and JMJD2D (KDM4D). We conclude by examining these findings in the context of related KMTs and KDMs and by exploring unresolved questions regarding the specificities and functions of these enzymes.

MATERIALS
Product Number
Brand
Product Description

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