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Nucleosome interaction surface of linker histone H1c is distinct from that of H1(0)

Academic Article
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Overview

authors

  • George, E. M.
  • Izard, T.
  • Anderson, S. D.
  • Brown, D. T.

publication date

  • 2010

journal

  • Journal of Biological Chemistry  Journal

abstract

  • The fully organized structure of the eukaryotic nucleosome remains unsolved, in part due to limited information regarding the binding site of the H1 or linker histone. The central globular domain of H1 is believed to interact with the nucleosome core at or near the dyad and to bind at least two strands of DNA. We utilized site-directed mutagenesis and in vivo photobleaching to identify residues that contribute to the binding of the globular domain of the somatic H1 subtype H1c to the nucleosome. As was previously observed for the H1(0) subtype, the binding residues for H1c are clustered on the surface of one face of the domain. Despite considerable structural conservation between the globular domains of these two subtypes, the locations of the binding sites identified for H1c are distinct from those of H1(0). We suggest that the globular domains of these two linker histone subtypes will bind to the nucleosome with distinct orientations that may contribute to higher order chromatin structure heterogeneity or to differences in dynamic interactions with other DNA or chromatin-binding proteins.

subject areas

  • Binding Sites
  • Chromatin
  • DNA
  • Gene Expression Regulation
  • Genes, Reporter
  • Green Fluorescent Proteins
  • Histones
  • Kinetics
  • Models, Molecular
  • Molecular Conformation
  • Mutagenesis
  • Mutagenesis, Site-Directed
  • Nucleosomes
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Identity

PubMed Central ID

  • PMC2898364

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M110.108639

PubMed ID

  • 20444700
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Additional Document Info

start page

  • 20891

end page

  • 20896

volume

  • 285

issue

  • 27

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