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Structural basis for retroviral integration into nucleosomes

Author

Listed:
  • Daniel P. Maskell

    (Chromatin Structure and Mobile DNA, The Francis Crick Institute)

  • Ludovic Renault

    (Architecture and Dynamics of Macromolecular Machines, Clare Hall Laboratories, The Francis Crick Institute
    National Institute for Biological Standards and Control, Microscopy and Imaging)

  • Erik Serrao

    (Dana-Farber Cancer Institute)

  • Paul Lesbats

    (Chromatin Structure and Mobile DNA, The Francis Crick Institute)

  • Rishi Matadeen

    (NeCEN, Gorlaeus Laboratory)

  • Stephen Hare

    (Imperial College London
    †Present address: Division of Molecular Biosciences, Imperial College London, South Kensington Campus, London SW7 2AZ, UK)

  • Dirk Lindemann

    (Institute of Virology, Technische Universität Dresden)

  • Alan N. Engelman

    (Dana-Farber Cancer Institute)

  • Alessandro Costa

    (Architecture and Dynamics of Macromolecular Machines, Clare Hall Laboratories, The Francis Crick Institute)

  • Peter Cherepanov

    (Chromatin Structure and Mobile DNA, The Francis Crick Institute
    Imperial College London)

Abstract

Retroviruses such as HIV rely on the intasome, a tetramer of integrase protein bound to the viral DNA ends interacting with host chromatin, for integration into the host genome; the structure of the intasome as it interacts with a nucleosome is now solved, giving insight into the integration process.

Suggested Citation

  • Daniel P. Maskell & Ludovic Renault & Erik Serrao & Paul Lesbats & Rishi Matadeen & Stephen Hare & Dirk Lindemann & Alan N. Engelman & Alessandro Costa & Peter Cherepanov, 2015. "Structural basis for retroviral integration into nucleosomes," Nature, Nature, vol. 523(7560), pages 366-369, July.
    • Handle: RePEc:nat:nature:v:523:y:2015:i:7560:d:10.1038_nature14495
    DOI: 10.1038/nature14495
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    Citations

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    Cited by:

    1. Hannah O. Ajoge & Tyler M. Renner & Kasandra Bélanger & Matthew Greig & Samar Dankar & Hinissan P. Kohio & Macon D. Coleman & Emmanuel Ndashimye & Eric J. Arts & Marc-André Langlois & Stephen D. Barr, 2023. "Antiretroviral APOBEC3 cytidine deaminases alter HIV-1 provirus integration site profiles," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    2. Li Wang & Jiali Yu & Zishuo Yu & Qianmin Wang & Wanjun Li & Yulei Ren & Zhenguo Chen & Shuang He & Yanhui Xu, 2022. "Structure of nucleosome-bound human PBAF complex," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    3. Guillermo Abascal-Palacios & Laura Jochem & Carlos Pla-Prats & Fabienne Beuron & Alessandro Vannini, 2021. "Structural basis of Ty3 retrotransposon integration at RNA Polymerase III-transcribed genes," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    4. Gayan Senavirathne & James London & Anne Gardner & Richard Fishel & Kristine E. Yoder, 2023. "DNA strand breaks and gaps target retroviral intasome binding and integration," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    5. Allison Ballandras-Colas & Vidya Chivukula & Dominika T. Gruszka & Zelin Shan & Parmit K. Singh & Valerie E. Pye & Rebecca K. McLean & Gregory J. Bedwell & Wen Li & Andrea Nans & Nicola J. Cook & Hind, 2022. "Multivalent interactions essential for lentiviral integrase function," Nature Communications, Nature, vol. 13(1), pages 1-16, December.

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