Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

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

http://www.ncbi.nlm.nih.gov/pubmed/16980972

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

Research resources used in this publication

None found

Research tools detected in this publication

None found

Data used in this publication

None found

Associated grants

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

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.