EzrA's QNR domain is sufficient to inhibit FtsZ assembly <i>in vitro</i>.

<p>(A) Data from 90°-angle light scattering experiments examining the impact of different EzrA constructs on FtsZ assembly <i>in vitro</i>. FtsZ is 5 µM in all reactions. Bars represent the maximum scatter averaged across three independent experiments with standard deviation at the top. Note that the small QNR fusion protein is a significantly more potent inhibitor of FtsZ assembly than the almost full length EzrA (27–562) fusion. EzrA refers to an N-terminal Thioredoxin fusion to EzrA (27–562) with a C-terminal 6XHis tag, while QNR refers to the last 69 residues of EzrA fused in the same orientation to Thioredoxin and 6XHis. QNR(R510D) includes a mutation in the QNR motif of the 69 residue construct that disrupts EzrA localization to midcell <i>in vivo </i><a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0102616#pone.0102616-Haeusser2" target="_blank">[7]</a>. Thio refers to the Thioredoxin-6XHis control protein. Bars equal standard deviation from three repeated experiments. (B) Representative trace of data from a 90°-angle light scattering reaction indicating the dose dependent nature of QNR mediated inhibition of FtsZ assembly. A.U. refers to arbitrary units.