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A thermodynamic model for Nap1-histone interactions.

The yeast nucleosome assembly protein 1 (yNap1) plays a role in chromatin maintenance by facilitating histone exchange as well as nucleosome assembly and disassembly. It has been suggested that yNap1 carries out these functions by regulating the concentration of free histones. Therefore, a quantitative understanding of yNap1-histone interactions also provides information on the thermodynamics of chromatin. We have developed quantitative methods to study the affinity of yNap1 for histones. We show that yNap1 binds H2A/H2B and H3/H4 histone complexes with low nm affinity, and that each yNap1 dimer binds two histone fold dimers. The yNap1 tails contribute synergistically to histone binding while the histone tails have a slightly repressive effect on binding. The (H3/H4)(2) tetramer binds DNA with higher affinity than it binds yNap1.

Pubmed ID: 18728017

Authors

  • Andrews AJ
  • Downing G
  • Brown K
  • Park YJ
  • Luger K

Journal

The Journal of biological chemistry

Publication Data

November 21, 2008

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM067777
  • Agency: NIGMS NIH HHS, Id: R01 GM067777
  • Agency: NIGMS NIH HHS, Id: R01 GM067777-06
  • Agency: Howard Hughes Medical Institute, Id:
  • Agency: Howard Hughes Medical Institute, Id:

Mesh Terms

  • Animals
  • Cell Cycle Proteins
  • Chromatin
  • DNA
  • Dimerization
  • Gene Expression Regulation, Fungal
  • Histones
  • Kinetics
  • Models, Biological
  • Nuclear Proteins
  • Nucleosome Assembly Protein 1
  • Protein Binding
  • Protein Folding
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Thermodynamics
  • Xenopus laevis