Key Laboratory of Plant Hormones and Development Regulation of Chongqing, School of Life Sciences, Chongqing University, 401331, Chongqing, China; Center of Plant Functional Genomics, Institute of Advanced Interdisciplinary Studies, Chongqing University, 401331, Chongqing, China; Institute of Agricultural Quality Standard and Testing Technology, Chongqing Academy of Agricultural Sciences, 401329, Chongqing, China.
Key Laboratory of Plant Hormones and Development Regulation of Chongqing, School of Life Sciences, Chongqing University, 401331, Chongqing, China; Center of Plant Functional Genomics, Institute of Advanced Interdisciplinary Studies, Chongqing University, 401331, Chongqing, China.
J Plant Physiol. 2021 Mar-Apr;258-259:153373. doi: 10.1016/j.jplph.2021.153373. Epub 2021 Feb 20.
Calmodulin-like proteins (CMLs), as well as their targets, play significant roles in various key developmental and stress responses in the plant. In tomato (Solanum lycopersicum), there are at least 52 CML genes in its genome. However, most of their functions are not well known, especially in response to cold stress. Here, we investigated SlCML37 biochemical and structural characteristics, including a typical α-helical secondary structure and exposing its hydrophobic regions after binding to Ca. Then we certificated that SlCML37 protein could physically interact with SlUMP1 by using yeast two-hybrid, bimolecular florescence complementation (BiFC) and GST pull-down assays. Further analysis showed that SlCML37-transgenic tomato fruit conferred significantly improved tolerance to chilling stress. This study indicates a possible role of calmodulin-like protein-mediated proteasome assemble in the regulation of plant cold response.
钙调素样蛋白（CMLs）及其靶标在植物的各种关键发育和应激反应中发挥重要作用。在番茄（Solanum lycopersicum）中，其基因组中至少有 52 个 CML 基因。然而，它们的大多数功能并不为人所知，特别是在应对冷胁迫时。在这里，我们研究了 SlCML37 的生化和结构特征，包括典型的α-螺旋二级结构，并在与 Ca 结合后暴露其疏水区。然后，我们通过酵母双杂交、双分子荧光互补（BiFC）和 GST 下拉实验证明 SlCML37 蛋白可以与 SlUMP1 发生物理相互作用。进一步的分析表明，SlCML37 转基因番茄果实对冷藏胁迫具有显著的耐受性。本研究表明钙调素样蛋白介导的蛋白酶体组装在植物冷响应调节中的可能作用。
