Biochemical and structural properties of heterochromatin protein 1: understanding its role in chromatin assembly.

Gohei Nishibuchi, Jun-ichi Nakayama

Journal: Journal of biochemistry 2015;156(1):11-20

PMID: 24825911

Abstract

Heterochromatin protein 1 (HP1) is an evolutionarily conserved chromosomal protein that binds lysine 9-methylated histone H3 (H3K9me), a hallmark of heterochromatin, and plays a crucial role in forming higher-order chromatin structures. HP1 has an N-terminal chromodomain and a C-terminal chromo shadow domain, linked by an unstructured hinge region. Although biochemical and structural studies have revealed each domain's properties, little is known about the mechanisms by which these domains cooperate to carry out HP1's function in forming higher-order chromatin structures. In this review, we summarize HP1's biochemical and structural properties and highlight the latest findings regarding HP1's interactions with nucleosomes.

© The Authors 2014. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

Address: Graduate School of Natural Sciences, Nagoya City University, Nagoya 467-8501, Japan.; Graduate School of Natural Sciences, Nagoya City University, Nagoya 467-8501, Japan [email protected].
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