Histone H3 Tail Modifications Alter Structure and Dynamics of the H1 C-Terminal Domain Within Nucleosomes |
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| Institution: | 1. Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, United States;2. Department of Biochemistry and Biophysics, Rochester University Medical Center, Rochester, NY 14625, United States;1. National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China;2. University of Chinese Academy of Sciences, Beijing 100049, China;3. Institute of Molecular Physiology, Shenzhen Bay Laboratory, Shenzhen 518132, China;4. School of Medicine, Sun Yat-sen University, Shenzhen 518107, China;5. Ministry of Education (MOE) Key Laboratory of Bioinformatics, School of Life Sciences, Tsinghua University, Beijing, China;6. Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, TaiKang Center for Life and Medical Sciences, Wuhan University, Wuhan 430072, China;1. Department of Molecular, Cellular, and Developmental Biology, University of Colorado Boulder, Boulder, CO 80303, United States;2. Department of Biochemistry, University of Colorado Boulder, Boulder, CO 80309, United States;3. Howard Hughes Medical Institute, Chevy Chase, MD 20815, United States;1. Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA;2. Center for Eukaryotic Gene Regulation, The Pennsylvania State University, University Park, PA 16802, USA;3. Department of Biomedical Sciences, University of North Dakota School of Medicine and Health Sciences, Grand Forks, ND 58201, USA;4. Department of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, FL 32610, USA;5. UF Health Cancer Center, University of Florida, Gainesville, FL 32610, USA;6. Department of Physics, The Pennsylvania State University, University Park, PA 16802, USA;1. Biophysics Graduate Program, The Ohio State University, Columbus, OH 43210, USA;2. Department of Biochemistry and Molecular Biology, Center for Eukaryotic Gene Regulation, The Pennsylvania State University, University Park, PA 16802, USA;3. Department of Physics, The Ohio State University, Columbus, OH 43210, USA;4. Huck Institutes of the Life Sciences, The Pennsylvania State University, University Park, PA 16802, USA;5. Department of Physics, The Pennsylvania State University, University Park, PA 16802, USA;6. Department of Chemistry & Biochemistry, The Ohio State University, Columbus, OH 43210, USA;1. School of Molecular Biosciences, Washington State University, Pullman, WA 99164, USA;2. Department of Chemistry and Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30303, USA;3. Center for Reproductive Biology, Washington State University, Pullman, WA 99164, USA;1. Max Planck Institute for Multidisciplinary Sciences, Department of Molecular Biology, Am Fassberg 11, 37077 Göttingen, Germany |
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| Abstract: | The highly positively charged and intrinsically disordered H1 C-terminal domain (CTD) undergoes extensive condensation upon binding to nucleosomes, and stabilizes nucleosomes and higher-order chromatin structures but its interactions in chromatin are not well defined. Using single-molecule FRET we found that about half of the H1 CTDs in H1-nucleosome complexes exhibit well-defined FRET values indicative of distinct, static conformations, while the remainder of the population exhibits exchange between multiple defined FRET structures. Moreover, crosslinking studies indicate that the first 30 residues of the H1 CTD participate in relatively localized contacts with the first ∼25 bp of linker DNA, and that two separate regions in the CTD contribute to H1-dependent organization of linker DNA. Finally, we show that acetylation mimetics within the histone H3 tail markedly reduce the overall extent of H1 CTD condensation and significantly increase the fraction of H1 CTDs undergoing dynamic exchange between FRET states. Our results indicate the nucleosome-bound H1 CTD adopts loosely defined structures that exhibit significantly enhanced dynamics and decondensation upon epigenetic acetylation within the H3 tail. |
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| Keywords: | Linker Histone H1 nucleosomes Intrinsically discorded protein single-molecule FRET histone acetylation |
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