Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2017 May 8;45(11):6644–6655. doi: 10.1093/nar/gkx357

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

PMC Copyright notice

Figure 7. — In vitro mutagenesis analysis of the role of conserved residues of Muta1 transposase in transposition. (A) DNA binding assay using wild-type and mutant transposases. Diagram shows the structure of the DNA substrate. The unlabeled 165-bp DNA containing 20-bp flanking DNA and the full length Muta1 L-TIR is added in 100 (+) molar excess as competitor DNA. Binding products are resolved on a native polyacrylamide gel. (B) Cleavage assay using wild-type and mutant transposases. Diagram shows the structure of DNA substrates and predicted cleavage product. Reaction products are resolved on a native polyacrylamide gel. (C) End joining assay using wild-type and mutant transposases. Intact pUC19 plasmid is used as target DNA. Reaction products are resolved on a native agarose gel.