Structural basis of seamless excision and specific targeting by piggyBac transposase

Structural basis of seamless excision and specific targeting by piggyBac transposase

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 transpos...

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Main Authors: Qiujia Chen, Wentian Luo, Ruth Ann Veach, Alison B. Hickman, Matthew H. Wilson, Fred Dyda
Format: Article
Language:English
Published: Nature Publishing Group 2020-07-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-020-17128-1
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spelling doaj-73fcb349e4bd4561984b0e66066d51962021-07-11T11:45:08ZengNature Publishing GroupNature Communications2041-17232020-07-0111111410.1038/s41467-020-17128-1Structural basis of seamless excision and specific targeting by piggyBac transposaseQiujia Chen0Wentian Luo1Ruth Ann Veach2Alison B. Hickman3Matthew H. Wilson4Fred Dyda5Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of HealthDepartment of Medicine, Division and Nephrology and Hypertension, Vanderbilt University Medical CenterDepartment of Medicine, Division and Nephrology and Hypertension, Vanderbilt University Medical CenterLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of HealthDepartment of Medicine, Division and Nephrology and Hypertension, Vanderbilt University Medical CenterLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of HealthPiggyBac 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.https://doi.org/10.1038/s41467-020-17128-1
collection DOAJ
language English
format Article
sources DOAJ
author Qiujia Chen
Wentian Luo
Ruth Ann Veach
Alison B. Hickman
Matthew H. Wilson
Fred Dyda
spellingShingle Qiujia Chen
Wentian Luo
Ruth Ann Veach
Alison B. Hickman
Matthew H. Wilson
Fred Dyda
Structural basis of seamless excision and specific targeting by piggyBac transposase
Nature Communications
author_facet Qiujia Chen
Wentian Luo
Ruth Ann Veach
Alison B. Hickman
Matthew H. Wilson
Fred Dyda
author_sort Qiujia Chen
title Structural basis of seamless excision and specific targeting by piggyBac transposase
title_short Structural basis of seamless excision and specific targeting by piggyBac transposase
title_full Structural basis of seamless excision and specific targeting by piggyBac transposase
title_fullStr Structural basis of seamless excision and specific targeting by piggyBac transposase
title_full_unstemmed Structural basis of seamless excision and specific targeting by piggyBac transposase
title_sort structural basis of seamless excision and specific targeting by piggybac transposase
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2020-07-01
description 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.
url https://doi.org/10.1038/s41467-020-17128-1
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AT wentianluo structuralbasisofseamlessexcisionandspecifictargetingbypiggybactransposase
AT ruthannveach structuralbasisofseamlessexcisionandspecifictargetingbypiggybactransposase
AT alisonbhickman structuralbasisofseamlessexcisionandspecifictargetingbypiggybactransposase
AT matthewhwilson structuralbasisofseamlessexcisionandspecifictargetingbypiggybactransposase
AT freddyda structuralbasisofseamlessexcisionandspecifictargetingbypiggybactransposase
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