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Asf1 is required for viability and chromatin assembly during DNA replication in vertebrate cells.

Author information

Affiliations

  • 1. Section of Biochemistry and Molecular Biology, Department of Medical Sciences, Miyazaki Medical College, University of Miyazaki, 5200 Kihara, Kiyotake, Miyazaki 889-1692, Japan.
      Authors
    • Sanematsu F 1
    • Takami Y 1
    • Barman HK 1
    (3 authors)
  • 2. Department of Molecular Genetics, National Institute of Genetics, 1111 Yata, Mishima, Shizuoka 411-8540, Japan.
      Authors
    • Fukagawa T 2
    (1 author)
  • 3. Department of Integrated Genetics, National Institute of Genetics, 1111 Yata, Mishima, Shizuoka 411-8540, Japan.
      Authors
    • Ono T 3
    • Shibahara KI 3
    (2 authors)
  • 4. Section of Biochemistry and Molecular Biology, Department of Medical Sciences, Miyazaki Medical College, University of Miyazaki, 5200 Kihara, Kiyotake, Miyazaki 889-1692, Japan; Department of Life Science, Frontier Science Research Center, University of Miyazaki, 5200, Kihara, Kiyotake, Miyazaki 889-1692, Japan.
      Authors
    • Nakayama T 4
    (1 author)

The Journal of Biological Chemistry, 14 Mar 2006, 281(19):13817-13827
https://doi.org/10.1074/jbc.m511590200 PMID: 16537536 

Abstract 

Asf1 (anti-silencing function 1), a well conserved protein from yeast to humans, acts as a histone chaperone and is predicted to participate in a variety of chromatin-mediated cellular processes. To investigate the physiological role of vertebrate Asf1 in vivo, we generated a conditional Asf1-deficient mutant from chicken DT40 cells. Induction of Asf1 depletion resulted in the accumulation of cells in S phase with decreased DNA replication and increased mitotic aberrancy forming multipolar spindles, leading to cell death. In addition, nascent chromatin in Asf1-depleted cells showed increased nuclease sensitivity, indicating impaired nucleosome assembly during DNA replication. Complementation analyses revealed that the functional domain of Asf1 for cell viability was confined to the N-terminal core domain (amino acids 1-155) that is a binding platform for histones H3/H4, CAF-1p60, and HIRA, whereas Asf1 mutant proteins, abolishing binding abilities with both p60 and HIRA, exhibit no effect on viability. These results together indicate that the vertebrate Asf1 plays a crucial role in replication-coupled chromatin assembly, cell cycle progression, and cellular viability and provide a clue of a possible role in a CAF-1- and HIRA-independent chromatin-modulating process for cell proliferation.

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Read article at publisher's site: https://doi.org/10.1074/jbc.m511590200

Read article for free, from open access legal sources, via Unpaywall: http://www.jbc.org/article/S0021925819749229/pdfUnpaywall

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