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. 2020 Jan 28;10:1383. doi: 10.1038/s41598-020-58395-8

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Investigation of OsHSP20 homodimerization in yeast cells. (A) Schematic representation of OsHSP20 and the five truncations generated in the study. The full-length OsHSP20 (Full; spanning residues 1 to 158) was divided into three parts: the N-terminal arm (N; spanning residues 1 to 52), the α-crystallin domain (ACD; residues 52 to 143) and the C-terminal extension region (C; residues 143 to 158). Five truncated forms of OsHSP20 were prepared to express N, ACD, C, N + ACD or ACD + C. The presence (+) or absence (−) of homodimerization in YTH assay is shown on the right. (B) Interaction of intact OsHSP20 and truncations of OsHSP20 in co-transformed yeast cells grown on SD/-Ade/-His/-Leu/-Trp/X-α-Gal/AbA medium. Yeast colonies expressing BD-53/AD-T were used as the positive control. Yeast co-transformed with BD-Lam/AD-T, BD-OsHSP20^Full/AD or BD/AD-OsHSP20^Full were used as negative controls.