Mechanisms and functions of protein S-acylation modifications at the plant vacuolar membrane

蛋白质s -酰化是一种重要的二次修饰，调控着蛋白质膜的结合、靶向和功能。然而，修饰蛋白s -酰基转移酶（PATs）和修饰靶蛋白的详细生化和遗传分析一直受到修饰酶对靶标功能冗余的阻碍。在植物中，蛋白质s -酰化的机制、功能和需求尚不清楚。因此，我们采用了功能筛选方法，从拟南芥中鉴定了一个特定的酶-底物对（PAT10-CBL2），现在可以直接解决植物叶绿体脂质修饰的机制。因此，本项目旨在阐明拟南芥中PAT蛋白10和11的功能特性，这两个蛋白代表了叶绿体定位酶。此外，我们将分析酶（PAT）及其底物的靶向所需的机制原理，特别是空泡PAT酶对底物（如细胞体结合的钙调磷酸酶b样（CBL）蛋白）的特异性修饰。

Protein S-acylation is an important secondary modification and regulates protein membrane association, targeting and function. However, detailed biochemical and genetic analyses of the modifying protein S-acyltransferases (PATs) and of modified target proteins have been hampered by the functional redundancy of modifying enzymes towards targets. In plants, the mechanisms, functions and requirements for protein S-acylation are not well understood. Therefore, we employed a functional screen and identified a specific enzyme-substrate pair (PAT10-CBL2) from Arabidopsis thaliana, which now allows addressing the mechanism of lipid modification at the plant tonoplast directly. Consequently, this project aims to elucidate the functional properties of the PAT proteins 10 and 11 from Arabidopsis, representing tonoplast localized enzymes. In addition we will analyze the mechanistic principles required for the targeting of enzymes (PAT) as well as their substrates, and especially the specific modification of substrates like the tonoplast bound calcineurin B-like (CBL) proteins by the vacuolar PAT enzymes.