F-type ATP synthases are multiprotein complexes composed of two separate coupled motors (F1 and FO) generating adenosine triphosphate (ATP) as the universal major energy source in a variety of relevant biological processes in mitochondria, bacteria and chloroplasts. In the past decades, ATP synthases have become a subject of high interest, as a target for therapeutic use in the treatment of a variety of diseases. While the structure of many ATPases is solved today, the precise assembly pathway

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... f F1FO-ATP synthases is mostly still unclear. To probe the bacterial F1 assembly of Acetobacterium woodii, we studied the self-assembly of purified proteins under different environments. We report assembly requirements, important assembly intermediates in vitro and in vivo, the crucial role of nucleotide binding (as opposed to ATP hydrolysis) and correlate results with complex activity. Finally, we propose a model for the assembly pathway for the formation of a functional F1 complex.