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. 2021 Jun 11;21:268. doi: 10.1186/s12870-021-03045-y

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© The Author(s) 2021

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 7 — The enzyme activity of cICDH depends on BRS1. a Total extractable ICDH activity from wild type (WS2 and Col-0) seedlings and a range of mutant lines: brs1-1D, brs1-1 and icdh-2. Means and SD of eight independent extracts are shown. Asterisks indicate a statistically significant difference based on Student’s t-test (*p < 0.05). b Subcellular localization of BRS1. Root tips from transgenic Col-0 plants expressing 35S-BRS1-GFP were used to visualize the subcellular localization of BRS1-GFP by confocal microscopy. The green fluorescence indicates the BRS1-GFP and the red fluorescence indicates propidium iodide staining. The merge channel represents the merge of BRS1-GFP and propidium iodide staining. Scale bar = 20 μm