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  Histone octamer rearranges to adapt to DNA unwrapping

Bilokapic, S., Strauss, M., & Halic, M. (2018). Histone octamer rearranges to adapt to DNA unwrapping. Nature Structural and Molecular Biology, 25(1), 101-108. doi:10.1038/s41594-017-0005-5.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0000-B180-6 Version Permalink: http://hdl.handle.net/21.11116/0000-0000-B182-4
Genre: Journal Article

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 Creators:
Bilokapic, Silvija1, Author
Strauss, Mike2, Author              
Halic, Mario1, Author
Affiliations:
1external, ou_persistent22              
2Scientific Service Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565170              

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Free keywords: NUCLEOSOME CORE PARTICLE; RNA-POLYMERASE-II; CRYSTAL-STRUCTURE; H2A/H2B DIMER; CRYO-EM; ACCESSIBILITY; TRANSCRIPTION; PURIFICATION; RESOLUTION; STABILITYBiochemistry & Molecular Biology; Biophysics; Cell Biology;
 Abstract: Nucleosomes, the basic units of chromatin, package and regulate expression of eukaryotic genomes. Although the structure of the intact nucleosome is well characterized, little is known about structures of partially unwrapped, transient intermediates. In this study, we present nine cryo-EM structures of distinct conformations of nucleosome and subnucleo-some particles. These structures show that initial DNA breathing induces conformational changes in the histone octamer, particularly in histone H3, that propagate through the nucleosome and prevent symmetrical DNA opening. Rearrangements in the H2A-H2B dimer strengthen interaction with the unwrapping DNA and promote nucleosome stability. In agreement with this, cross-linked H2A-H2B that cannot accommodate unwrapping of the DNA is not stably maintained in the nucleosome. H2A-H2B release and DNA unwrapping occur simultaneously, indicating that DNA is essential in stabilizing the dimer in the nucleosome. Our structures reveal intrinsic nucleosomal plasticity that is required for nucleosome stability and might be exploited by extrinsic protein factors.

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Language(s): eng - English
 Dates: 2018
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: ISI: 000423547700014
DOI: 10.1038/s41594-017-0005-5
 Degree: -

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Title: Nature Structural and Molecular Biology
  Other : Nature Struct Biol
Source Genre: Journal
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Publ. Info: New York, NY : Nature Pub. Group
Pages: - Volume / Issue: 25 (1) Sequence Number: - Start / End Page: 101 - 108 Identifier: ISSN: 1545-9993
CoNE: https://pure.mpg.de/cone/journals/resource/954925603763