Structural Paradigms in the Recognition of the Nucleosome Core Particle by Histone Lysine Methyltransferases

Ashley Janna; Hossein Davarinejad; Monika Joshi; Jean-Francois Couture

doi:10.3389/fcell.2020.00600

Structural Paradigms in the Recognition of the Nucleosome Core Particle by Histone Lysine Methyltransferases

Front Cell Dev Biol. 2020 Jul 31:8:600. doi: 10.3389/fcell.2020.00600. eCollection 2020.

Authors

Ashley Janna¹, Hossein Davarinejad¹, Monika Joshi¹, Jean-Francois Couture¹

Affiliation

¹ Ottawa Institute of Systems Biology, Shanghai Institute of Materia Medica-University of Ottawa Research Center in Systems and Personalized Pharmacology, Department of Biochemistry, Microbiology and Immunology, University of Ottawa, Ottawa, ON, Canada.

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.

Keywords: chromatin; epigenetics; histone; methylation; ubiquitinylation.

Publication types

Review