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Intrinsic elasticity of nucleosomes is encoded by histone variants and calibrated by their binding partners

Histone variants fine-tune transcription, replication, DNA damage repair, and faithful chromosome segregation. Whether and how nucleosome variants encode unique mechanical properties to their cognate chromatin structures remains elusive. Here, using in silico and in vitro nanoindentation methods, ex...

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Published in:	Proceedings of the National Academy of Sciences - PNAS 2019-11, Vol.116 (48), p.24066-24074
Main Authors:	Melters, Daniël P., Pitman, Mary, Rakshit, Tatini, Dimitriadis, Emilios K., Bui, Minh, Papoian, Garegin A., Dalal, Yamini
Format:	Article
Language:	English
Subjects:	Adaptability Binding Biological Sciences Centromere Protein A - chemistry Chromatin Chromosomal Proteins, Non-Histone - chemistry Chromosome Segregation Chromosomes Computer Simulation Deoxyribonucleic acid DNA DNA biosynthesis DNA damage DNA Repair DNA Replication Elasticity Histones Histones - chemistry Histones - physiology In vitro methods and tests In vivo methods and tests Mechanical properties Molecular Dynamics Simulation Nanoindentation Nucleosomes Nucleosomes - chemistry Nucleosomes - physiology Protein Structure, Tertiary Proteins Transcription Transcription, Genetic
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creator	Melters, Daniël P. Pitman, Mary Rakshit, Tatini Dimitriadis, Emilios K. Bui, Minh Papoian, Garegin A. Dalal, Yamini
description	Histone variants fine-tune transcription, replication, DNA damage repair, and faithful chromosome segregation. Whether and how nucleosome variants encode unique mechanical properties to their cognate chromatin structures remains elusive. Here, using in silico and in vitro nanoindentation methods, extending to in vivo dissections, we report that histone variant nucleosomes are intrinsically more elastic than their canonical counterparts. Furthermore, binding proteins, which discriminate between histone variant nucleosomes, suppress this innate elasticity and also compact chromatin. Interestingly, when we overexpress the binding proteins in vivo, we also observe increased compaction of chromatin enriched for histone variant nucleosomes, correlating with diminished access. Taken together, these data suggest a plausible link between innate mechanical properties possessed by histone variant nucleosomes, the adaptability of chromatin states in vivo, and the epigenetic plasticity of the underlying locus.
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subjects	Adaptability Binding Biological Sciences Centromere Protein A - chemistry Chromatin Chromosomal Proteins, Non-Histone - chemistry Chromosome Segregation Chromosomes Computer Simulation Deoxyribonucleic acid DNA DNA biosynthesis DNA damage DNA Repair DNA Replication Elasticity Histones Histones - chemistry Histones - physiology In vitro methods and tests In vivo methods and tests Mechanical properties Molecular Dynamics Simulation Nanoindentation Nucleosomes Nucleosomes - chemistry Nucleosomes - physiology Protein Structure, Tertiary Proteins Transcription Transcription, Genetic
title	Intrinsic elasticity of nucleosomes is encoded by histone variants and calibrated by their binding partners
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