Bacterial F-type ATP synthases follow a well-choreographed assembly pathway.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 35260553.
- Also identified by DOI 10.1038/s41467-022-28828-1 and PMC identifier 8904574.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
F-type ATP synthases are multiprotein complexes composed of two separate coupled motors (F<sub>1</sub> and F<sub>O</sub>) generating adenosine triphosphate (ATP) as the universal major energy source in a variety of relevant biological processes in mitochondria, bacteria and chloroplasts. While the structure of many ATPases is solved today, the precise assembly pathway of F<sub>1</sub>F<sub>O</sub>-ATP synthases is still largely unclear. Here, we probe the assembly of the F<sub>1</sub> complex from Acetobacterium woodii. Using laser induced liquid bead ion desorption (LILBID) mass spectrometry, we study the self-assembly of purified F<sub>1</sub> subunits in different environments under non-denaturing conditions. We report assembly requirements and identify important assembly intermediates in vitro and in cellula. Our data provide evidence that nucleotide binding is crucial for in vitro F<sub>1</sub> assembly, whereas ATP hydrolysis appears to be less critical. We correlate our results with activity measurements and propose a model for the assembly pathway of a functional F<sub>1</sub> complex.
Medical subject headings
- Adenosine Triphosphate
- Mitochondrial Proton-Translocating ATPases