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

Franka Voigt, Lisa Wiedemann, Cecilia Zuliani, Irma Querques, Attila Sebe, Lajos Mátés, Zsuzsanna Izsvák, Zoltán Ivics and Orsolya Barabas ()
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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
Zsuzsanna Izsvák: Max Delbrück Center for Molecular Medicine
Zoltán Ivics: Paul Ehrlich Institute
Orsolya Barabas: European Molecular Biology Laboratory, Structural and Computational Biology Unit

Nature Communications, 2016, vol. 7, issue 1, 1-8

Abstract: 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.

Date: 2016
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DOI: 10.1038/ncomms11126

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