Structural insights into the histone H1-nucleosome complex

Linker H1 histones facilitate formation of higher-order chromatin structures and play important roles in various cell functions. Despite several decades of effort, the structural basis of how H1 interacts with the nucleosome remains elusive. Here, we investigated Drosophila H1 in complex with the nu...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 110; no. 48; pp. 19390 - 19395
Main Authors Zhou, Bing-Rui, Feng, Hanqiao, Kato, Hidenori, Dia, Liang, Yang, Yuedong, Zhou, Yaoqi, Bai, Yawen
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 26.11.2013
NATIONAL ACADEMY OF SCIENCES
National Acad Sciences
Subjects
Amino Acid Sequence
Biochemistry
Biological Sciences
Biophysics
Calorimetry
Chromatin
Deoxyribonucleic acid
DNA
Drosophila
Genetic mutation
Histones
Histones - chemistry
Histones - genetics
Insects
Macromolecular Substances - chemistry
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Conformation
Molecular Sequence Data
Mutagenesis, Site-Directed
NMR
Nuclear magnetic resonance
Nucleic acids
Nucleosomes
Nucleosomes - chemistry
Protein Binding
Proteins
Spectrum analysis
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Summary:Linker H1 histones facilitate formation of higher-order chromatin structures and play important roles in various cell functions. Despite several decades of effort, the structural basis of how H1 interacts with the nucleosome remains elusive. Here, we investigated Drosophila H1 in complex with the nucleosome, using solution nuclear magnetic resonance spectroscopy and other biophysical methods. We found that the globular domain of H1 bridges the nucleosome core and one 10-base pair linker DNA asymmetrically, with its α3 helix facing the nucleosomal DNA near the dyad axis. Two short regions in the C-terminal tail of H1 and the C-terminal tail of one of the two H2A histones are also involved in the formation of the H1–nucleosome complex. Our results lead to a residue-specific structural model for the globular domain of the Drosophila H1 in complex with the nucleosome, which is different from all previous experiment-based models and has implications for chromatin dynamics in vivo.
Bibliography:http://dx.doi.org/10.1073/pnas.1314905110
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Author contributions: B.-R.Z. and Y.B. designed research; B.-R.Z., H.F., L.D., Y.Y., and Y.Z. performed research; H.K. contributed new reagents/analytic tools; B.-R.Z., H.F., L.D., Y.Y., Y.Z., and Y.B. analyzed data; and B.-R.Z. and Y.B. wrote the paper.
Edited by S. Walter Englander, The University of Pennsylvania, Philadelphia, PA, and approved October 22, 2013 (received for review August 6, 2013)
1Present address: Institute for Glycomics and School of Informatics and Communication Technology, Griffith University, Southport, QLD 4222, Australia.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1314905110