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Structural basis for recognition of H3K56-acetylated histone H3–H4 by the chaperone Rtt106

Author

Listed:
  • Dan Su

    (Mayo Clinic)

  • Qi Hu

    (Mayo Clinic)

  • Qing Li

    (Mayo Clinic)

  • James R. Thompson

    (Mayo Clinic)

  • Gaofeng Cui

    (Mayo Clinic)

  • Ahmed Fazly

    (Mayo Clinic)

  • Brian A. Davies

    (Mayo Clinic)

  • Maria Victoria Botuyan

    (Mayo Clinic)

  • Zhiguo Zhang

    (Mayo Clinic)

  • Georges Mer

    (Mayo Clinic)

Abstract

Direct binding of Rtt106 to H3K56-acetylated (H3–H4)2 histone tetramers contributes to nucleosome assembly with implications for DNA replication, gene silencing and maintenance of genomic stability.

Suggested Citation

  • Dan Su & Qi Hu & Qing Li & James R. Thompson & Gaofeng Cui & Ahmed Fazly & Brian A. Davies & Maria Victoria Botuyan & Zhiguo Zhang & Georges Mer, 2012. "Structural basis for recognition of H3K56-acetylated histone H3–H4 by the chaperone Rtt106," Nature, Nature, vol. 483(7387), pages 104-107, March.
    • Handle: RePEc:nat:nature:v:483:y:2012:i:7387:d:10.1038_nature10861
    DOI: 10.1038/nature10861
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