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

. 2014 May 31;42(12):7935–7946. doi: 10.1093/nar/gku494

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

© The Author(s) 2014. 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/3.0/), 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. — The relaxation of negatively supercoiled pUC19 plasmid by ScTopA is dependent on its C-terminal domain. (A) Agarose gel-based assay demonstrating rapid appearance of low-density topoisomers produced by ScTopA even at low protein concentration (25–50 nM; lanes 1 and 2). (B) Comparison of processive and distributive removal of supercoils during the reaction sustained by wild-type ScTopA (100 nM) and mutant ScTopA881 truncated in C-terminus by 71 amino acids (100 nM), respectively. (C) Estimation of kinetic parameters V_max and K_m by fitting to the Michaelis–Menten equation for wild-type ScTopA and mutant ScTopA881. (D) Deletion of C-terminal domain (343 aa) completely abolishes the activity of the ScTopAΔC mutant (700 nM).