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...

Full description

Saved in:
Bibliographic Details
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
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1911880116