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级修饰，调节蛋白质膜结合、靶向和功能。然而，修饰蛋白S-酰基转移酶（PAT）和修饰的靶蛋白的详细的生物化学和遗传分析已受到阻碍的修饰酶对目标的功能冗余。在植物中，蛋白质S-酰化的机制、功能和要求尚不清楚。因此，我们采用了功能筛选，并确定了一个特定的酶底物对（PAT 10-CBL 2）从拟南芥，现在允许解决的机制，脂质修饰在植物液泡膜直接。因此，本项目旨在阐明拟南芥PAT蛋白10和11的功能特性，代表液泡膜定位酶。此外，我们将分析所需的靶向酶（PAT）以及其底物的机械原理，特别是特异性修饰的液泡膜结合的钙调磷酸酶B样（CBL）蛋白质的液泡PAT酶的底物。

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.