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. 2015 Sep 9;10(9):e0137439. doi: 10.1371/journal.pone.0137439

Fig 1. The optimal and core DNA-binding domains of EIN3.

Fig 1

(A) A Schematic model for EIN3 action in multiple signaling pathways. (B) Schematic structural diagram of full length and truncated EIN3 proteins. Acidic region, coil region, proline-rich region, basic domains, and asparagine-rich domain are represented by different color filled boxes. Highly conserved regions are also indicated by red boxes. (C) Representative EMSA results of different EIN3 truncations binding to a 3’–biotin labeled ERF1 probe. Specific EIN3 truncations used for each lane are shown in the upper panel and the fraction bound is shown in the lower panel. EIN3 114–352 displayed minimal binding under the current protein concentration, yet clearly bound to DNA at higher concentration (S3C Fig). In addition, the same amount of different EIN3 truncations was used in each PAGE-gel in order to have better visual comparisons, and similar results were obtained at other concentrations of proteins (S3A Fig). “B”: bound; “F”: free. (D) Relative binding data for 0.2 μM truncated EIN3 proteins with ERF1. The data were normalized to the fraction bound of 82–352 with ERF1; error bars represented the standard deviation from three independent experiments. (E) EMSA results of the core DBD (174–306), which retained the ability to bind to ERF1.