EMSA using 212 300 and the PRC2 3m complex showed a similar affinity to that found for EZH2-EED binding (Kd = 111 ± 10 nM for PRC2 vs 135 ± 20 nM for EZH2-EED), indicating that the binding interaction was not an artifact arising from the more minimal EZH2-EED heterodimer.
Functional studies have suggested interactions with the nuclear export protein CRM1 [ 50], although direct binding interactions were not demonstrated in that study.
However, given that the first acidic region, STDE, of hTFIIEα has no effect on the binding, the interaction is not merely based on electrostatic interactions.
pH drop had no effect on CusA binding to Ni2+, confirming that the interaction is not mediated by histidine but rather by methionine as it has been previously proposed [5].
Although the actual mechanism facilitating peroxisome acto-myosin interaction is not known, binding of RhoA-GTP to the peroxisomal membrane may trigger this process possibly by activating NMM IIA.
Furthermore, FRET between the BD-C2 mutated channel constructs and YFP-apoCaM was negligible (2.6±2.2%, n = 9), verifying that the interaction is not due to binding of Ca2+-unbound CaM.
In the case that an interaction did not have at least one DNA binding domain, this interaction was not considered.
However, whether BAK1 acts as a regulator or co-receptor of BRI1 and how BR binding promotes BRI1-BAK1 interareionotre not well understood.
A reliable calculation of the binding affinity for this interaction was not possible because saturation of GST-IgFLNa20 21 GST-IgFLNa20 21ould not bindingeved.
