---
res:
  bibo_abstract:
  - 'The HIRA histone chaperone complex is comprised of four protein subunits: HIRA,
    UBN1, CABIN1, and transiently associated ASF1a. All four subunits have been demonstrated
    to play a role in the deposition of the histone variant H3.3 onto areas of actively
    transcribed euchromatin in cells. The mechanism by which these subunits function
    together to drive histone deposition has remained poorly understood. Here we present
    biochemical and biophysical data supporting a model whereby ASF1a delivers histone
    H3.3/H4 dimers to the HIRA complex, H3.3/H4 tetramerization drives the association
    of two HIRA/UBN1 complexes, and the affinity of the histones for DNA drives release
    of ASF1a and subsequent histone deposition. These findings have implications for
    understanding how other histone chaperone complexes may mediate histone deposition.@eng'
  bibo_authorlist:
  - foaf_Person:
      foaf_givenName: Austin
      foaf_name: Vogt, Austin
      foaf_surname: Vogt
  - foaf_Person:
      foaf_givenName: Mary
      foaf_name: Szurgot, Mary
      foaf_surname: Szurgot
  - foaf_Person:
      foaf_givenName: Lauren
      foaf_name: Gardner, Lauren
      foaf_surname: Gardner
      foaf_workInfoHomepage: http://www.librecat.org/personId=f9dedd98-6d15-11f0-88a5-a7b4143fdec5
    orcid: 0009-0000-5733-1546
  - foaf_Person:
      foaf_givenName: David C.
      foaf_name: Schultz, David C.
      foaf_surname: Schultz
  - foaf_Person:
      foaf_givenName: Ronen
      foaf_name: Marmorstein, Ronen
      foaf_surname: Marmorstein
  bibo_doi: 10.1016/j.jbc.2024.107604
  bibo_issue: '9'
  bibo_volume: 300
  dct_date: 2024^xs_gYear
  dct_isPartOf:
  - http://id.crossref.org/issn/0021-9258
  - http://id.crossref.org/issn/1083-351X
  dct_language: eng
  dct_publisher: Elsevier@
  dct_title: HIRA complex deposition of histone H3.3 is driven by histone tetramerization
    and histone-DNA binding@
  fabio_hasPubmedId: '39059488'
...