Emma Buzzard, Mathew McLaren, Piotr Bragoszewski, Andrea Brancaccio, Holly Ford, Bertram Daum, Patricia Kuwabara, Ian Collinson, Vicki Gold
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引用次数: 0
Abstract
Mitochondrial ATP synthases form rows of dimers, which induce membrane curvature to give cristae their characteristic lamellar or tubular morphology. The angle formed between the central stalks of ATP synthase dimers varies between species. Using cryo-electron tomography and sub-tomogram averaging, we determined the structure of the ATP synthase dimer from the nematode worm C. elegans and show that the dimer angle differs from previously determined structures. The consequences of this species-specific difference at the dimer interface were investigated by comparing C. elegans and S. cerevisiae mitochondrial morphology. We reveal that C. elegans has a larger ATP synthase dimer angle with more lamellar (flatter) cristae when compared to yeast. The underlying cause of this difference was investigated by generating an atomic model of the C. elegans ATP synthase dimer by homology modelling. A comparison of our C. elegans model to an existing S. cerevisiae structure reveals the presence of extensions and rearrangements in C. elegans subunits associated with maintaining the dimer interface. We speculate that increasing dimer angles could provide an advantage for species that inhabit variable-oxygen environments by forming flatter more energetically efficient cristae.
线粒体 ATP 合成酶形成成排的二聚体,这些二聚体促使膜弯曲,从而使嵴呈现出特有的片状或管状形态。ATP 合成酶二聚体中心柄之间形成的角度因物种而异。利用低温电子断层扫描和子图平均法,我们确定了线虫C. elegans的ATP合成酶二聚体的结构,并表明二聚体的角度与之前确定的结构不同。通过比较线虫和麦角虫的线粒体形态,我们研究了二聚体界面上这种物种特异性差异的后果。我们发现,与酵母相比,秀丽隐杆线粒体的 ATP 合酶二聚体角度更大,嵴的片状(扁平)更多。我们通过同源建模生成了优雅子 ATP 合酶二聚体的原子模型,从而研究了造成这种差异的根本原因。将我们的秀丽隐杆线虫模型与现有的 S. cerevisiae 结构进行比较后发现,秀丽隐杆线虫亚基中存在与维持二聚体界面相关的延伸和重排。我们推测,增加二聚体角度可以形成更扁平、能量效率更高的嵴,从而为栖息在变氧环境中的物种提供优势。
期刊介绍:
Exploring the molecular mechanisms that underpin key biological processes, the Biochemical Journal is a leading bioscience journal publishing high-impact scientific research papers and reviews on the latest advances and new mechanistic concepts in the fields of biochemistry, cellular biosciences and molecular biology.
The Journal and its Editorial Board are committed to publishing work that provides a significant advance to current understanding or mechanistic insights; studies that go beyond observational work using in vitro and/or in vivo approaches are welcomed.
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Cell biology
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