Multi-omic profiling of histone variant H3.3 lysine 27 methylation reveals a distinct role from canonical H3 in stem cell differentiation

Author:

Kori Yekaterina1ORCID,Lund Peder J.2,Trovato Matteo34ORCID,Sidoli Simone5ORCID,Yuan Zuo-Fei6,Noh Kyung-Min3,Garcia Benjamin A.2ORCID

Affiliation:

1. Epigenetics Institute, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA

2. Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA

3. European Molecular Biology Laboratory (EMBL), Genome Biology Unit, Heidelberg, Germany

4. Collaboration for Joint PhD Degree between EMBL and Heidelberg University, Faculty of Biosciences, Heidelberg, Germany

5. Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, USA

6. Center for Proteomics and Metabolomics, St. Jude Children's Research Hospital, Memphis, TN 38105, USA

Abstract

Post-translational modifications on histone variants may differ from their canonical counterparts. We investigate the role of lysine 27 tri-methylation on the histone variant H3.3 in the context of stem cell pluripotency and differentiation.

Funder

National Institutes of Health

Blavatnik Family Foundation

Publisher

Royal Society of Chemistry (RSC)

Subject

Genetics,Molecular Biology,Biochemistry

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