TY  - JOUR
AU  - Voigt, Franka
AU  - Wiedemann, Lisa
AU  - Zuliani, Cecilia
AU  - Querques, Irma
AU  - Sebe, Attila
AU  - Mátés, Lajos
AU  - Izsvák, Zsuzsanna
AU  - Ivics, Zoltán
AU  - Barabas, Orsolya
TI  - Sleeping Beauty transposase structure allows rational design of hyperactive variants for genetic engineering
JO  - Nature Communications
VL  - 7
SN  - 2041-1723
CY  - London
PB  - Nature Publishing Group
M1  - PUBDB-2016-06025
SP  - 11126 
PY  - 2016
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000373291300001
C6  - pmid:27025571
DO  - DOI:10.1038/ncomms11126
UR  - https://bib-pubdb1.desy.de/record/315679
ER  -