Tomato calmodulin-like protein SlCML37 is a calcium (Ca2+ ) sensor that interacts with proteasome maturation factor SlUMP1 and plays a role in tomato fruit chilling stress tolerance

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 alpha-helical secondary structure and exposing its hydrophobic regions after binding to Ca2+. 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.

Automated summary

Calmodulin-like proteins and their interactions with targets play an important role in plant responses to stress. In this study, the biochemical characteristics of SlCML37 were investigated, and it was found to improve tolerance to chilling stress in tomato fruit through physical interaction with SlUMP1.