Transposase makes critical contacts with, and is stimulated by, single-stranded DNA at the P element termini in vitro

The EMBO Journal
E L Beall, Donald C Rio

Abstract

P elements transpose by a cut-and-paste mechanism. Donor DNA cleavage mediated by transposase generates 17 nucleotide (nt) 3' single-strand extensions at the P element termini which, when present on oligonucleotide substrates, stimulate both the strand-transfer and disintegration reactions in vitro. A significant amount of the strand-transfer products are the result of double-ended integration. Chemical DNA modification-interference experiments indicate that during the strand-transfer reaction, P element transposase contacts regions of the substrate DNA that include the transposase binding site and the duplex portion of the 31 bp inverted repeat, as well as regions of the terminal 17 nt single-stranded DNA. Together these data suggest that the P element transposase protein contains two DNA-binding sites and that the active oligomeric form of the transposase protein is at least a dimer.

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Citations

Sep 25, 2003·Insect Biochemistry and Molecular Biology·K MichelP W Atkinson
Nov 9, 2007·Journal of Molecular Biology·Kathryn M LembergTania A Baker
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Nov 2, 2016·Proceedings of the National Academy of Sciences of the United States of America·Malik Joseph FrancisDonald C Rio
Jul 24, 2007·The Journal of Biological Chemistry·Mei TangDonald C Rio
Oct 30, 2019·Nature Structural & Molecular Biology·George E GhanimDonald C Rio
Dec 23, 2020·Open Biology·George E GhanimFelipe Karam Teixeira
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Jun 25, 2015·Microbiology Spectrum·Sharmistha Majumdar, Donald C Rio
Jun 25, 2015·Microbiology Spectrum·Alison B Hickman, Fred Dyda

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