课题基金 / 基金详情

Coordination Funds

Coordination Funds
协调基金
批准号:
524931683
负责人:
Professor Dr. Michael Hippler
金额:
$0.0万
依托单位国家:
德国
项目类别:
Research Units
财政年份:
--
资助国家:
德国
项目状态:
未结题
起止时间:
关键词:

项目摘要

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中文摘要
翻译
质子动力(PMF)是能量代谢的核心,为大多数细胞功能提供燃料。它是普遍的遗传密码,并一直在塑造进化。PMF是跨膜的电化学梯度,通常由多个膜蛋白复合物协同活动产生。它将能量转换从分子身份和化学计量约束中分离出来,自由地连接和整合其他不相关的细胞过程。这一特性是PMF成功的关键。在特别灵活的同时,PMF还必须严格可靠地为生化反应提供燃料并维持细胞。为了保证能量供应,必须将环境和生理刺激整合到PMF调节中。尽管人们对PMF进行了深入研究,但对监管策略的理解仍然不够充分。最近,功能成像和生物传感技术揭示了线粒体PMF的新颖基本特征。虽然这些见解已经开始改变我们对生物能量动力学的理解范式,但对含氧光合作用却缺乏类似的见解。然而,在光合作用的背景下研究PMF特别适合作为理解PMF动力学基础原理的一种方法,因为它特别容易受到自然栖息地光线波动的快速外部变化的影响。该研究小组(GoPMF)将研究如何在多变的自然环境中调节PMF的产生和调节以优化光合作用的输出。在最近的发现和该计划成员的方法发展的推动下,我们将在亚细胞组织和生理学的背景下评估光合生物能量学。我们将利用蓝藻和叶绿体作为体内模型来剖析翻译后和生理水平上PMF快速调节的机制。这些见解将与产生和调节PMF的分子机器的机制和结构分析联系在一起。结合最先进的成像技术,随着原位生物传感技术的发展,监测PMF在单个细胞、细胞器和类囊体中的生物能量特征,将使我们对PMF管理的理解进入一个新的细胞生物学背景。通过快速时间分辨光谱、质谱和结构生物学(包括cryo-EM和cryo-ET),将获得驱动PMF动力学机制的机械分子细节。广泛的基因工程将利用蓝藻、藻类和植物对PMF调控的机制保护和多样性。这些功能研究将与PMF的数学建模相结合。我们希望将PMF理解为一个动态的,响应性的和集成的中心,它塑造了光合作用及其对快速外部变化的调整。
英文摘要
The proton motive force (PMF) is at the heart of energy metabolism and fuels most cellular functions. It is universal as the genetic code and has been shaping evolution. The PMF is an electrochemical gradient across a membrane, usually generated by the concerted activity of multiple membrane protein complexes. It separates energy transformation from molecular identities and stochiometric constraints and freely connects and integrates otherwise unrelated cellular processes. This feature has been key for the success of the PMF. While being particularly flexible, the PMF must also be strictly reliable to fuel biochemical reactions and to maintain the cell. To guarantee energy supply, environmental and physiological stimuli must be integrated into PMF regulation. Even though the PMF has been studied intensely, regulatory strategies remain insufficiently understood. Recently, functional imaging and biosensing techniques have uncovered novel, fundamental features of the mitochondrial PMF. While those insights have started to shift the paradigms of our understanding of bioenergetic dynamics, similar insights are lacking for oxygenic photosynthesis. Yet, studying PMF in the context of photosynthesis is particularly well suited as an approach to understand the principles underpinning PMF dynamics, because it is particularly prone to rapid external changes due to fluctuating light in natural habitats. This Research Group (GoPMF) will develop concepts of how the generation and modulation of the PMF is regulated to optimize photosynthetic output in changeable natural environments. Driven by recent discoveries and enabling methodological developments by members of this initiative, we will assess photosynthetic bioenergetics within its context of subcellular organization and physiology. We will make use of cyanobacteria and chloroplasts as in vivo models to dissect mechanisms of rapid PMF adjustment at the posttranslational and physiological level. These insights will be linked with mechanistic and structural analyses of the molecular machines that generate and modulate the PMF. Combining state-of-the-art imaging techniques, with the development of in situ biosensing techniques to monitor bioenergetic characteristics of the PMF live in individual cells, organelles and thylakoids will take our understanding of PMF management into a novel cell biological context. Mechanistic molecular detail into the mechanisms driving PMF dynamics will be gained through fast time-resolved spectroscopy, mass spectrometry and structural biology including cryo-EM and cryo-ET. Extensive genetic engineering will take advantage of the mechanistic conservation and diversity in PMF regulation by cyanobacteria, algae and plants. These functional studies will be flanked by mathematical modeling of the PMF. We expect to establish an understanding of the PMF as a dynamic, responsive and integrated hub that shapes photosynthesis and its adjustment to rapid external changes.
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会议论文
Central proteomic platform for the Research Unit
Calcium-dependent regulation of photosynthesis in Chlamydomonas reinhardtii: Structural and functional dynamics of calredoxin, a chloroplast Ca2+-dependent thioredoxin
Mechanistic insights into the function of the ancient light-harvesting protein LHCSR3 in light energy dissipation in Chlamydomonas reinhardtii
Central Project 2_Central proteomic platform for the Research Unit
海外基金