Chloroplast metalloproteinase SlL2 reduces the thermotolerance of tomato by decreasing the content of SlCDJ1.

Abstract

Chloroplast is one of the most sensitive organelles to heat stress in plants. In chloroplasts, various proteases affect photosynthesis by degrading proteins under stress conditions. Tomato Lutescent2 (SlL2), a chloroplast zinc metalloprotease, was previously reported to alter chloroplast development and delay fruit ripening. However, its enzyme activity and roles in plant response to abiotic stress are still unclear. Here, we confirmed that the SlL2 protein which localized on thylakoid membrane was an ATP-independent hydrolase, and SlL2 gene responded to heat stress. Phenotype analysis showed that SlL2 plays a negative role in the heat-response mechanism. Under heat stress, the transgenic plants overexpressing SlL2 (OE) grew worse than the wild type (WT), as reflected by their decreased membrane stability, osmotic-regulating substance, and antioxidative enzyme activities, as well as increased reactive oxygen species (ROS) accumulation. By contrast, l2 mutant line showed the opposite phenotype and corresponding physiological indices under heat stress. In addition, overexpression of SlL2 decreased the photosynthetic activities, especially photosystem II. Moreover, SlL2 was found to interact with chloroplast-located chaperone protein SlCDJ1, decreasing its content under heat stress. These results indicate that SlL2 reduces the thermotolerance of tomato by reducing the content of SlCDJ1.