Abstract
Post-translational modifications (PTMs) of histone proteins play essential functions in shaping chromatin environment. Alone or in combination, these PTMs create templates recognized by dedicated proteins or change the chemistry of chromatin, enabling a myriad of nuclear processes to occur. Referred to as cross-talk, the positive or negative impact of a PTM on another PTM has rapidly emerged as a mechanism controlling nuclear transactions. One of those includes the stimulatory functions of histone H2B ubiquitylation on the methylation of histone H3 on K79 and K4 by Dot1L and COMPASS, respectively. While these findings were established early on, the structural determinants underlying the positive impact of H2B ubiquitylation on H3K79 and H3K4 methylation were resolved only recently. We will also review the molecular features controlling these cross-talks and the impact of H3K27 tri-methylation on EZH2 activity when embedded in the PRC2 complex.
Highlights
LYSINE METHYLATIONProtein lysine methylation involves the transfer of up to three methyl groups to the -amine of a lysine residue
THE NUCLEOSOMEThe genetic material of a typical eukaryotic cell approximately measures 2 meters and must be restricted to the confines of the nucleus
The findings suggest that the presence of ubiquitin may alter the dynamics of the catalytic subunit in alleviating an auto-inhibitory function of the SET1 Arginine Rich Motif (ARM) motif (Hsu et al, 2019)
Summary
Protein lysine methylation involves the transfer of up to three methyl groups to the -amine of a lysine residue. Methylation of a lysine residue was first reported by Ambler and Rees (1959) in the flagellin protein of Salmonella typhimurium These findings, further led by additional studies on histone H1, H3, and H4 lysine methylation (Couture and Trievel, 2006; Lee et al, 2010), unveiled that this post-translational modification (PTM) fine-tunes the activity of transcription factors (Yang et al, 2009), participates in the assembly of multisubunit complexes (Zhang et al, 2005; Donlin et al, 2012), and contributes to the structural organization of chromosomes (Lanouette et al, 2014). They are extremely specific and, in most cases, have the ability to recognize a single lysine side chain on a single protein (Lanouette et al, 2014)
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