Format

Send to

Choose Destination
Nat Struct Mol Biol. 2019 Nov;26(11):1013-1022. doi: 10.1038/s41594-019-0319-6. Epub 2019 Oct 28.

Structure of a P element transposase-DNA complex reveals unusual DNA structures and GTP-DNA contacts.

Author information

1
Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA, USA.
2
California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, CA, USA.
3
California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, CA, USA. ehk68@cornell.edu.
4
Molecular Biology and Genetics Department, Cornell University, Ithaca, NY, USA. ehk68@cornell.edu.
5
Howard Hughes Medical Institute, University of California, Berkeley, Berkeley, CA, USA.
6
Molecular Biophysics and Integrative Bio-Imaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
7
Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA, USA. don_rio@berkeley.edu.
8
California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, CA, USA. don_rio@berkeley.edu.

Abstract

P element transposase catalyzes the mobility of P element DNA transposons within the Drosophila genome. P element transposase exhibits several unique properties, including the requirement for a guanosine triphosphate cofactor and the generation of long staggered DNA breaks during transposition. To gain insights into these features, we determined the atomic structure of the Drosophila P element transposase strand transfer complex using cryo-EM. The structure of this post-transposition nucleoprotein complex reveals that the terminal single-stranded transposon DNA adopts unusual A-form and distorted B-form helical geometries that are stabilized by extensive protein-DNA interactions. Additionally, we infer that the bound guanosine triphosphate cofactor interacts with the terminal base of the transposon DNA, apparently to position the P element DNA for catalysis. Our structure provides the first view of the P element transposase superfamily, offers new insights into P element transposition and implies a transposition pathway fundamentally distinct from other cut-and-paste DNA transposases.

PMID:
31659330
DOI:
10.1038/s41594-019-0319-6

Supplemental Content

Full text links

Icon for Nature Publishing Group
Loading ...
Support Center