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. 2020 Oct 29;21(21):8070. doi: 10.3390/ijms21218070

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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The RsRplA interacts with a plant cathepsin. (a) Pairwise yeast-two-hybrid analysis between RsRlpA (used as a prey in pGADT7 vector) and potentially interacting plant proteases (used as baits in pGBKT7 vector). Growth of yeast cells on SD-4 (-His, -Ade, -Leu, -Trp) selective media represents protein–protein interaction and growth on SD-2 (-Leu, -Trp) media confirms yeast transformation. Yeasts transformed with the empty vectors were used as negative controls. (b) Co-immunoprecipitation (co-IP) assay between the GFP-tagged RsRlpA and HA-tagged cathepsin, transiently co-expressed in N. benthamiana and pull-downed using the GFP-trap agarose magnetic beads.