Interaction between MED19a and HaRxL44 is important for HaRxL44–induced MED19a degradation via proteasome.

Abstract

<p>(A) Immunoblotting of proteins, extracted from <i>N. benthamiana</i> leaves after transient assay. Note the absence of Co-IP of HA-HaRxL44<sup>M</sup> with GFP-MED19a. (B) Co-localisation analysis between GFP-MED19a and RFP-HaRxL44 or HaRxL44<sup>M</sup> determined by transient assay in <i>N. benthamiana</i>. Note the lack of GFP-MED19a in the presence of RFP-HaRxL44 (arrow) but not HaRxL44<sup>M</sup>. (C) Quantification of the number of fluorescent nucleoplasm observed in nucleus transformed with GFP-MED19a in the presence or not of RFP-HaRxL44 or RFP-HaRxL44<sup>M</sup>. All the confocal pictures were taken with PMT 1 (494–541 nm) at Gain: 864 and PMT 2 (591–649 nm) at Gain: 844. Note the decrease in GFP-MED19a transformed cells in the presence of RFP-HaRxL44 in comparison with RFP alone or RFP-HaRxL44<sup>M</sup>.</p

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