Auxiliary factors required for the accumulation and functioning of the thylakoid ATP Synthase

类囊体中的F1 Fo-ATP脱氢酶将ATP合成与光驱动的电化学质子梯度偶联。F1 Fo-ATP酶是无辅因子的多蛋白复合物，由跨膜结构域（CFo）和外周结构域（CF 1）组成。目前对类囊体ATP合酶的形成知之甚少，只有少数组装因子被鉴定。在以前的工作中，我们可以确定拟南芥中的类囊体整合蛋白CGL 160（AtCGL 160），这是所需的高效CFo组装。AtCGL 160包含两个结构域;植物特异性结构域和与蓝藻蛋白Atp 1远亲的第二个结构域。此外，我们可以确定一个额外的新的推定类囊体ATP合成酶组装因子在拟南芥：AtHTN 1。该子项目的目的是在分子水平上破译AtHTN 1和植物特异性AtCGL 160结构域在ATP合酶组装中的功能。我们还将扩展我们的研究，在集胞藻Atp 1的功能特性和分析其在蓝藻ATP合酶组装过程中的作用，遗传，生化和电子显微镜的方法。我们的长期目标是阐明构建功能性类囊体ATP合酶所必需的整个辅助因子集合的相互作用，以确定它们的作用模式并解开它们功能的进化。

F1Fo-ATP synthases in thylakoids couple ATP synthesis to the light-driven electrochemical proton gradient. F1Fo-ATP synthases are cofactor-free multiprotein complexes and consist of a membrane-spanning (CFo) and a peripheral domain (CF1). Relatively little is known about thylakoid ATP synthase formation and only few assembly factors have been characterized so far. In previous work we could identify the thylakoid integral protein CGL160 in Arabidopsis (AtCGL160), which is required for efficient CFo assembly. AtCGL160 contains two domains; a plant-specific domain and a second domain which is distantly related to the cyanobacterial protein Atp1. Moreover, we could identify an additional novel putative thylakoid ATP synthase assembly factor in Arabidopsis: AtHTN1. The objective of this subproject is to decipher the function of AtHTN1 and of the plant-specific AtCGL160 domain in ATP synthase assembly at the molecular level. We will also extend our study to the functional characterization of Atp1 in Synechocystis and analyze its role in the cyanobacterial ATP synthase assembly process by genetic, biochemical and electron microscopy approaches. Our long-term goal is to elucidate the interplay of the entire ensemble of auxiliary factors necessary to construct a functional thylakoid ATP synthase, to determine their mode of action and to unravel the evolution of their function(s).