The LeATL6-associated ubiquitin/proteasome system may contribute to fungal elicitor-activated defense response via the jasmonic acid-dependent signaling pathway in tomato
The expression of LeATL6, an ortholog of Arabidopsis ATL6 that encodes a diamond ring-H2 finger protein, was caused in tomato roots given a cell wall protein fraction (CWP) elicitor from the biocontrol agent Pythium oligandrum. The LeATL6 protein was expressed like a fusion protein having a maltose-binding protein (MBP) in Escherichia coli, also it catalyzed the change in ubiquitin towards the MBP moiety on incubation with ubiquitin, the ubiquitin-activating enzyme E1, and also the ubiquitin-conjugating enzyme E2 this established that LeATL6 represents ubiquitin ligase E3. LeATL6 expression also was caused by elicitor management of jail-1 mutant tomato cells where the jasmonic acidity (JA)-mediated signaling path was impaired however, JA-dependent expression from the fundamental PR-6 and TPI-1 genes that encode proteinase inhibitor II and that i, correspondingly, wasn’t caused in elicitor-treated jail-1 mutants. In addition, transient overexpression of LeATL6 underneath the charge of the Cauliflower mosaic virus 35S promoter caused the fundamental PR6 and TPI-1 expression in wild tomato but away from the jail-1 mutant. In comparison, LeATL6 overexpression didn’t activate salicylic acidity-responsive acidic PR-1 and PR-2 promoters in wild tomato. These results established that elicitor-responsive LeATL6 most likely regulates JA-dependent fundamental PR6 and TPI-1 gene expression in tomato. The LeATL6-connected ubiquitin/proteasome system may lead to elicitor-activated defense responses using a JA-dependent signaling path in plants.