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HJURP uses distinct CENP-A surfaces to recognize and to stabilize CENP-A/histone H4 for centromere assembly.


Centromeres are defined by the presence of chromatin containing the histone H3 variant, CENP-A, whose assembly into nucleosomes requires the chromatin assembly factor HJURP. We find that whereas surface-exposed residues in the CENP-A targeting domain (CATD) are the primary sequence determinants for HJURP recognition, buried CATD residues that generate rigidity with H4 are also required for efficient incorporation into centromeres. HJURP contact points adjacent to the CATD on the CENP-A surface are not used for binding specificity but rather to transmit stability broadly throughout the histone fold domains of both CENP-A and H4. Furthermore, an intact CENP-A/CENP-A interface is a requirement for stable chromatin incorporation immediately upon HJURP-mediated assembly. These data offer insight into the mechanism by which HJURP discriminates CENP-A from bulk histone complexes and chaperones CENP-A/H4 for a substantial portion of the cell cycle prior to mediating chromatin assembly at the centromere.

Pubmed ID: 22406139


  • Bassett EA
  • DeNizio J
  • Barnhart-Dailey MC
  • Panchenko T
  • Sekulic N
  • Rogers DJ
  • Foltz DR
  • Black BE


Developmental cell

Publication Data

April 17, 2012

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM08275
  • Agency: NIGMS NIH HHS, Id: GM082989
  • Agency: NIGMS NIH HHS, Id: R01 GM082989
  • Agency: NIGMS NIH HHS, Id: R01 GM082989-01A1
  • Agency: NIGMS NIH HHS, Id: R01 GM082989-02
  • Agency: NIGMS NIH HHS, Id: R01 GM082989-03
  • Agency: NIGMS NIH HHS, Id: R01 GM082989-04
  • Agency: NIGMS NIH HHS, Id: T32 GM008136
  • Agency: NIGMS NIH HHS, Id: T32 GM008275

Mesh Terms

  • Amino Acid Sequence
  • Autoantigens
  • Binding Sites
  • Cell Cycle
  • Centromere
  • Chromatin Assembly and Disassembly
  • Chromosomal Proteins, Non-Histone
  • DNA-Binding Proteins
  • HeLa Cells
  • Histones
  • Humans
  • Immunoblotting
  • Mass Spectrometry
  • Molecular Sequence Data
  • Nucleosomes
  • Protein Binding
  • Protein Conformation
  • Recombinant Proteins
  • Sequence Homology, Amino Acid