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Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly.

Human HIRA, ASF1a, ASF1b and CAF-1 are evolutionally conserved histone chaperones that form multiple functionally distinct chromatin-assembly complexes, with roles linked to diverse nuclear process, such as DNA replication and formation of heterochromatin in senescent cells. We report the crystal structure of an ASF1a-HIRA heterodimer and a biochemical dissection of ASF1a's mutually exclusive interactions with HIRA and the p60 subunit of CAF-1. The HIRA B domain forms an antiparallel beta-hairpin that binds perpendicular to the strands of the beta-sandwich of ASF1a, via beta-sheet, salt bridge and van der Waals contacts. The N- and C-terminal regions of ASF1a and ASF1b determine the different affinities of these two proteins for HIRA, by contacting regions outside the HIRA B domain. CAF-1 p60 also uses B domain-like motifs for binding to ASF1a, thereby competing with HIRA. Together, these studies begin to define the molecular determinants of assembly of functionally diverse macromolecular histone chaperone complexes.

Pubmed ID: 16980972 RIS Download

Mesh terms: Amino Acid Sequence | Cell Cycle Proteins | Cell Line, Tumor | Histone Chaperones | Histones | Humans | Models, Molecular | Molecular Chaperones | Molecular Sequence Data | Protein Binding | Protein Structure, Tertiary | Sensitivity and Specificity | Structure-Activity Relationship | Transcription Factors | Transfection

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Associated grants

  • Agency: NIGMS NIH HHS, Id: R01 GM060293-01
  • Agency: NIGMS NIH HHS, Id: Y1 GM-0080-3
  • Agency: NIA NIH HHS, Id: P01 AG031862
  • Agency: NIA NIH HHS, Id: P01 AG031862-010001
  • Agency: NIGMS NIH HHS, Id: Y01 GM000080
  • Agency: NIGMS NIH HHS, Id: R01 GM060293

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