Structural basis of seamless excision and specific targeting by piggyBac transposase

Qiujia Chen; Wentian Luo; Ruth Ann Veach; Alison B. Hickman; Matthew H. Wilson; Fred Dyda

doi:10.1038/s41467-020-17128-1

Nature Communications (Jul 2020)

Structural basis of seamless excision and specific targeting by piggyBac transposase

Qiujia Chen,
Wentian Luo,
Ruth Ann Veach,
Alison B. Hickman,
Matthew H. Wilson,
Fred Dyda

Affiliations

Qiujia Chen: Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
Wentian Luo: Department of Medicine, Division and Nephrology and Hypertension, Vanderbilt University Medical Center
Ruth Ann Veach: Department of Medicine, Division and Nephrology and Hypertension, Vanderbilt University Medical Center
Alison B. Hickman: Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
Matthew H. Wilson: Department of Medicine, Division and Nephrology and Hypertension, Vanderbilt University Medical Center
Fred Dyda: Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health

DOI: https://doi.org/10.1038/s41467-020-17128-1
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 14

Abstract

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PiggyBac is a transposon used in genome engineering that does not leave excision footprints. Here the authors determine the structures of two complexes in which the piggyBac transposase is bound to DNA representing different steps of the transposition reaction, providing a basis for how the transposition reaction proceeds.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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