New players in heterochromatin silencing: histone variant H3.3 and the ATRX/DAXX chaperone

Hsiao P J Voon; Lee H Wong

doi:10.1093/nar/gkw012

New players in heterochromatin silencing: histone variant H3.3 and the ATRX/DAXX chaperone

Nucleic Acids Res. 2016 Feb 29;44(4):1496-501. doi: 10.1093/nar/gkw012. Epub 2016 Jan 14.

Authors

Hsiao P J Voon¹, Lee H Wong²

Affiliations

¹ Department of Biochemistry and Molecular Biology, The Biomedicine Discovery Institute, Monash University, Wellington Road, Clayton, Victoria 3800, Australia.
² Department of Biochemistry and Molecular Biology, The Biomedicine Discovery Institute, Monash University, Wellington Road, Clayton, Victoria 3800, Australia lee.wong@monash.edu.

Abstract

A number of studies have demonstrated that various components of the ATRX/DAXX/Histone H3.3 complex are important for heterochromatin silencing at multiple genomic regions. We provide an overview of the individual components (ATRX, DAXX and/or H3.3) tested in each study and propose a model where the ATRX/DAXX chaperone complex deposits H3.3 to maintain the H3K9me3 modification at heterochromatin throughout the genome.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Adaptor Proteins, Signal Transducing / genetics*
Chromatin Assembly and Disassembly / genetics
Co-Repressor Proteins
DNA Helicases / genetics*
Genome, Human
Heterochromatin / genetics*
Histone-Lysine N-Methyltransferase / genetics
Histones / genetics*
Humans
Molecular Chaperones / genetics
Multiprotein Complexes / genetics
Nuclear Proteins / genetics*
X-linked Nuclear Protein

Substances

Adaptor Proteins, Signal Transducing
Co-Repressor Proteins
DAXX protein, human
Heterochromatin
Histones
Molecular Chaperones
Multiprotein Complexes
Nuclear Proteins
Histone-Lysine N-Methyltransferase
DNA Helicases
ATRX protein, human
X-linked Nuclear Protein