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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.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Ghanim GE,Kellogg EH,Nogales E,Rio DC

doi

10.1038/s41594-019-0319-6

subject

Has Abstract

pub_date

2019-11-01 00:00:00

pages

1013-1022

issue

11

eissn

1545-9993

issn

1545-9985

pii

10.1038/s41594-019-0319-6

journal_volume

26

pub_type

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