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Sleeping Beauty transposase structure allows rational design of hyperactive variants for genetic engineering

Author

Listed:
  • Franka Voigt

    (European Molecular Biology Laboratory, Structural and Computational Biology Unit)

  • Lisa Wiedemann

    (Paul Ehrlich Institute)

  • Cecilia Zuliani

    (European Molecular Biology Laboratory, Structural and Computational Biology Unit)

  • Irma Querques

    (European Molecular Biology Laboratory, Structural and Computational Biology Unit)

  • Attila Sebe

    (Paul Ehrlich Institute)

  • Lajos Mátés

    (Max Delbrück Center for Molecular Medicine
    Present address: Biological Research Centre, Institute of Genetics, Temesvári krt. 62, Szeged 6726, Hungary.)

  • Zsuzsanna Izsvák

    (Max Delbrück Center for Molecular Medicine)

  • Zoltán Ivics

    (Paul Ehrlich Institute)

  • Orsolya Barabas

    (European Molecular Biology Laboratory, Structural and Computational Biology Unit)

Abstract

Sleeping Beauty (SB) is a prominent Tc1/mariner superfamily DNA transposon that provides a popular genome engineering tool in a broad range of organisms. It is mobilized by a transposase enzyme that catalyses DNA cleavage and integration at short specific sequences at the transposon ends. To facilitate SB’s applications, here we determine the crystal structure of the transposase catalytic domain and use it to model the SB transposase/transposon end/target DNA complex. Together with biochemical and cell-based transposition assays, our structure reveals mechanistic insights into SB transposition and rationalizes previous hyperactive transposase mutations. Moreover, our data enables us to design two additional hyperactive transposase variants. Our work provides a useful resource and proof-of-concept for structure-based engineering of tailored SB transposases.

Suggested Citation

  • Franka Voigt & Lisa Wiedemann & Cecilia Zuliani & Irma Querques & Attila Sebe & Lajos Mátés & Zsuzsanna Izsvák & Zoltán Ivics & Orsolya Barabas, 2016. "Sleeping Beauty transposase structure allows rational design of hyperactive variants for genetic engineering," Nature Communications, Nature, vol. 7(1), pages 1-8, September.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11126
    DOI: 10.1038/ncomms11126
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    Cited by:

    1. Alexander V. Shkumatov & Nicolas Aryanpour & Cédric A. Oger & Gérôme Goossens & Bernard F. Hallet & Rouslan G. Efremov, 2022. "Structural insight into Tn3 family transposition mechanism," Nature Communications, Nature, vol. 13(1), pages 1-12, December.

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