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. 2018 Jan 18;69(7):1485–1498. doi: 10.1093/jxb/ery001

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© The Author(s) 2018. Published by Oxford University Press on behalf of the Society for Experimental Biology.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Fig. 3. — Interactions of C1 and S1 proteins. (A) Schematic representation of the C1 protein domains. Boxes represent different C1 fragments used in yeast two-hybrid assays. C1^NIP represents protein from Nipponbare with the deletion of one glutamic acid in the R3 repeat. (B) Schematic representation of the S1 protein domains. (C) Yeast two-hybrid assays for C1 with S1. The pGADT7 and pGBKT7 plasmids contain the GAL4 activation and DNA-binding domains, respectively. C1 with intact protein or protein lacking one amino acid was fused to the pGADT7 plasmid and S1 with intact protein was fused to the pGBKT7 plasmid. The colony growth patterns at 3 and 8 d are shown. (D) Yeast two-hybrid assays for the interactions between truncated C1 and S1 proteins. C1 with intact protein or truncated proteins was fused to the pGADT7 plasmid and S1 with intact protein or its N-terminal domain was fused to the pGBKT7 plasmid.