Cathepsin B degrades RbcL during freezing-induced programmed cell death in Arabidopsis

• DOI: 10.1007/s00299-023-03099-2
• Publication Date: 2024-02-28T17:02:29Z
• Authors: Gang Yang; Tao Chen; Ting-ting Fan; Xiang-yu Lin; Yu-qiong Cui; Wei-chao Dong; Li-zhe An; Hua Zhang
• Keywords: 0301 basic medicine; 0303 health sciences; Arabidopsis Proteins; Ribulose-Bisphosphate Carboxylase; Freezing; Arabidopsis; Apoptosis; Cathepsin B

Abstract Programmed cell death (PCD) has been well documented in both development and in response to environmental stresses in plants; however, PCD induced by freezing stress and its molecular mechanisms remain poorly understood. In the present study, we characterised freezing-induced PCD and explored its mechanisms in Arabidopsis. PCD induced by freezing stress was similar to that induced by other stresses and senescence in Arabidopsis plants with cold acclimation. Inhibitor treatment assays and immunoblotting indicated that cathepsin B mainly contributed to increased caspase-3-like activity during freezing-induced PCD. Cathepsin B was involved in freezing-induced PCD and degraded the large subunit, RbcL, of Rubisco. Our results demonstrate an essential regulatory mechanism of cathepsin B for Rubisco degradation in freezing-induced PCD, improving our understanding of freezing-induced cell death and nitrogen and carbohydrate remobilisation in plants.