Unknown

Dataset Information

0

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


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.

SUBMITTER: Ghanim GE 

PROVIDER: S-EPMC6948148 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Ghanim George E GE   Kellogg Elizabeth H EH   Nogales Eva E   Rio Donald C DC  

Nature structural & molecular biology 20191028 11


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 nucleoprote  ...[more]

Similar Datasets

| S-EPMC5871717 | biostudies-literature
| S-EPMC2956205 | biostudies-literature
| S-EPMC2717000 | biostudies-literature
| S-EPMC3779457 | biostudies-literature
| S-EPMC3436135 | biostudies-literature
| S-EPMC1170234 | biostudies-other
2014-12-03 | E-GEOD-62534 | biostudies-arrayexpress
| S-EPMC5576353 | biostudies-literature
| S-EPMC2634953 | biostudies-literature
| S-EPMC6648845 | biostudies-literature