Nature Communications (Oct 2019)
Histone H3K23-specific acetylation by MORF is coupled to H3K14 acylation
- Brianna J. Klein,
- Suk Min Jang,
- Catherine Lachance,
- Wenyi Mi,
- Jie Lyu,
- Shun Sakuraba,
- Krzysztof Krajewski,
- Wesley W. Wang,
- Simone Sidoli,
- Jiuyang Liu,
- Yi Zhang,
- Xiaolu Wang,
- Becka M. Warfield,
- Andrew J. Kueh,
- Anne K. Voss,
- Tim Thomas,
- Benjamin A. Garcia,
- Wenshe R. Liu,
- Brian D. Strahl,
- Hidetoshi Kono,
- Wei Li,
- Xiaobing Shi,
- Jacques Côté,
- Tatiana G. Kutateladze
Affiliations
- Brianna J. Klein
- Department of Pharmacology, University of Colorado School of Medicine
- Suk Min Jang
- Laval University Cancer Research Center, CHU de Québec-UL Research Center-Oncology Division
- Catherine Lachance
- Laval University Cancer Research Center, CHU de Québec-UL Research Center-Oncology Division
- Wenyi Mi
- Center for Epigenetics, Van Andel Research Institute
- Jie Lyu
- Department of Biological Chemistry, University of California, Irvine
- Shun Sakuraba
- Molecular Modeling and Simulation Group, National Institute for Quantum Life Science, National Institutes for Quantum and Radiological Science and Technology
- Krzysztof Krajewski
- Department of Biochemistry & Biophysics, The University of North Carolina School of Medicine
- Wesley W. Wang
- Department of Chemistry, Texas A&M University
- Simone Sidoli
- Epigenetics Program, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania
- Jiuyang Liu
- Department of Pharmacology, University of Colorado School of Medicine
- Yi Zhang
- Department of Pharmacology, University of Colorado School of Medicine
- Xiaolu Wang
- Center for Epigenetics, Van Andel Research Institute
- Becka M. Warfield
- Department of Pharmacology, University of Colorado School of Medicine
- Andrew J. Kueh
- The Walter and Eliza Hall Institute of Medical Research
- Anne K. Voss
- The Walter and Eliza Hall Institute of Medical Research
- Tim Thomas
- The Walter and Eliza Hall Institute of Medical Research
- Benjamin A. Garcia
- Epigenetics Program, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania
- Wenshe R. Liu
- Department of Chemistry, Texas A&M University
- Brian D. Strahl
- Department of Biochemistry & Biophysics, The University of North Carolina School of Medicine
- Hidetoshi Kono
- Molecular Modeling and Simulation Group, National Institute for Quantum Life Science, National Institutes for Quantum and Radiological Science and Technology
- Wei Li
- Department of Biological Chemistry, University of California, Irvine
- Xiaobing Shi
- Center for Epigenetics, Van Andel Research Institute
- Jacques Côté
- Laval University Cancer Research Center, CHU de Québec-UL Research Center-Oncology Division
- Tatiana G. Kutateladze
- Department of Pharmacology, University of Colorado School of Medicine
- DOI
- https://doi.org/10.1038/s41467-019-12551-5
- Journal volume & issue
-
Vol. 10,
no. 1
pp. 1 – 13
Abstract
Acetylation of histone H3K23 has emerged as an essential posttranslational modification, yet this epigenetic mark remains poorly understood. Here, the authors identify the native MORF complex as a histone H3K23-specific acetyltransferase and show that interaction of the MORF subunit with acylated H3K14 promotes acetylation of H3K23 by this complex to activate transcription.
