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 t

SUBMITTER: Ghanim GE 

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

REPOSITORIES: biostudies-literature