P09 Structure and mechanisms of membrane protein complexes in mitochondrial membrane organization
P09 线粒体膜组织中膜蛋白复合物的结构和机制
基本信息
- 批准号:426717306
- 负责人:
- 金额:--
- 依托单位:
- 依托单位国家:德国
- 项目类别:Research Units
- 财政年份:2019
- 资助国家:德国
- 起止时间:2018-12-31 至 2022-12-31
- 项目状态:已结题
- 来源:
- 关键词:
项目摘要
In the present application, we will expand and intensify our cryoEM studies by adopting cryoET of focused ion-beam lamellae of flash-frozen unicellular organisms or mitochondria isolated from different cells and tissues to investigate open questions, in close collaboration with other consortium members. These questions include the distribution and mutual arrangement of the large membrane protein complexes that work as proton pumps and carry out ATP synthesis in the inner membrane cristae, as well as the sequence of events and sites of their assembly. We will resume our studies of how ageing affects mammalian mitochondria at the molecular level, with special attention to the ATP synthase dimers and respiratory chain supercomplexes. Finally, we will continue our successful collaboration on the structure and mechanisms of the dynamin-like mitochondrial GTPases to find out how they mediate mitochondrial dynamics and maintain the shape of mitochondrial cristae.
在本申请中,我们将与其他联盟成员密切合作,通过采用冷冻电子显微镜(cryoET)对闪冻单细胞生物或从不同细胞和组织分离的线粒体的聚焦离子束片层进行研究,来扩大和加强我们的冷冻电镜研究。这些问题包括作为质子泵并在内膜嵴中进行 ATP 合成的大型膜蛋白复合物的分布和相互排列,以及事件的顺序和它们的组装位点。我们将继续研究衰老如何在分子水平上影响哺乳动物线粒体,特别关注 ATP 合酶二聚体和呼吸链超复合物。最后,我们将继续在类似动力的线粒体 GTP 酶的结构和机制方面进行成功的合作,以找出它们如何介导线粒体动力学并维持线粒体嵴的形状。
项目成果
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Professor Dr. Werner Kühlbrandt其他文献
Professor Dr. Werner Kühlbrandt的其他文献
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