Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 107, Issue 4, Pages 1349-1354Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0913709107
Keywords
histone chaperone; histone variant
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Funding
- Centre National de la Recherche Scientifique
- Institut National de la Sante et de la Recherche Medicale
- ANR [NT05-1_41978, 08-BLAN-0320-02]
- INCA
- Association pour la Recherche sur le Cancer
- La fondation pour la Recherche Medicale
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The human histone H3 variant, CENP-A, replaces the conventional histone H3 in centromeric chromatin and, together with centromerespecific DNA-binding factors, directs the assembly of the kinetochore. We purified the prenucelosomal e-CENP-A complex. We found that HJURP, a member of the complex, was required for cell cycle specific targeting of CENP-A to centromeres. HJURP facilitated efficient deposition of CENP-A/H4 tetramers to naked DNA in vitro. Bacterially expressed HJURP binds at a stoichiometric ratio to the CENP-A/H4 tetramer but not to the H3/H4 tetramer. The binding occurred through a conserved HJURP short N-terminal domain, termed CBD. The novel characteristic identified in vertebrates that we named TLTY box of CBD, was essential for formation of the HJURP-CENP-A/H4 complex. Our data identified HJURP as a vertebrate CENP-A chaperone and dissected its mode of interactions with CENP-A.
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