Distinct roles for canonical and variant histone H3 lysine-36 in Polycomb silencing

Author:

Salzler Harmony R.1ORCID,Vandadi Vasudha1,McMichael Benjamin D.12ORCID,Brown John C.1ORCID,Boerma Sally A.3ORCID,Leatham-Jensen Mary P.1ORCID,Adams Kirsten M.2ORCID,Meers Michael P.14ORCID,Simon Jeremy M.56ORCID,Duronio Robert J.12456,McKay Daniel J.1245ORCID,Matera A. Gregory12456ORCID

Affiliation:

1. Integrative Program for Biological and Genome Sciences, University of North Carolina, Chapel Hill, NC, USA.

2. Department of Biology, University of North Carolina, Chapel Hill, NC, USA.

3. Department of Biology, Carleton College, Northfield, MN, USA.

4. Curriculum in Genetics and Molecular Biology, University of North Carolina, Chapel Hill, NC, USA.

5. Department of Genetics, University of North Carolina, Chapel Hill, NC, USA.

6. Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC, USA.

Abstract

Polycomb complexes regulate cell type–specific gene expression programs through heritable silencing of target genes. Trimethylation of histone H3 lysine 27 (H3K27me3) is essential for this process. Perturbation of H3K36 is thought to interfere with H3K27me3. We show that mutants of Drosophila replication-dependent ( H3.2 K36R ) or replication-independent ( H3.3 K36R ) histone H3 genes generally maintain Polycomb silencing and reach later stages of development. In contrast, combined ( H3.3 K36R H3.2 K36R ) mutants display widespread Hox gene misexpression and fail to develop past the first larval stage. Chromatin profiling revealed that the H3.2 K36R mutation disrupts H3K27me3 levels broadly throughout silenced domains, whereas these regions are mostly unaffected in H3.3 K36R animals. Analysis of H3.3 distributions showed that this histone is enriched at presumptive Polycomb response elements located outside of silenced domains but relatively depleted from those inside. We conclude that H3.2 and H3.3 K36 residues collaborate to repress Hox genes using different mechanisms.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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