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


Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
26 11 2019
Historique:
pubmed: 13 11 2019
medline: 23 4 2020
entrez: 13 11 2019
Statut: ppublish

Résumé

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.

Identifiants

pubmed: 31712435
pii: 1911880116
doi: 10.1073/pnas.1911880116
pmc: PMC6883791
doi:

Substances chimiques

Centromere Protein A 0
Chromosomal Proteins, Non-Histone 0
Histones 0
Nucleosomes 0
centromere protein C 0

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, N.I.H., Intramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

24066-24074

Informations de copyright

Copyright © 2019 the Author(s). Published by PNAS.

Déclaration de conflit d'intérêts

The authors declare no competing interest.

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Auteurs

Daniël P Melters (DP)

Laboratory Receptor Biology and Gene Expression, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892.

Mary Pitman (M)

Laboratory Receptor Biology and Gene Expression, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892.
Department of Chemistry and Biochemistry, Institute for Physical Science and Technology, University of Maryland, College Park, MD 20742.

Tatini Rakshit (T)

Laboratory Receptor Biology and Gene Expression, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892.

Emilios K Dimitriadis (EK)

Scanning Probe Microscopy Unit, Biomedical Engineering and Physical Science Shared Resource, National Institute for Biomedical Imaging and Bioengineering, National Institutes of Health, Bethesda, MD 20892.

Minh Bui (M)

Laboratory Receptor Biology and Gene Expression, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892.

Garegin A Papoian (GA)

Department of Chemistry and Biochemistry, Institute for Physical Science and Technology, University of Maryland, College Park, MD 20742; gpapoian@umd.edu dalaly@mail.nih.gov.

Yamini Dalal (Y)

Laboratory Receptor Biology and Gene Expression, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892; gpapoian@umd.edu dalaly@mail.nih.gov.

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Classifications MeSH