Bacterial F-type ATP synthases follow a well-choreographed assembly pathway
- 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. While the structure of many ATPases is solved today, the precise assembly pathway of F1FO-ATP synthases is still largely unclear. Here, we probe the assembly of the F1 complex from Acetobacterium woodii. Using laser induced liquid bead ion desorption (LILBID) mass spectrometry, we study the self-assembly of purified F1 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 F1 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 F1 complex.
Author: | Khanh Vu HuuORCiDGND, Rene ZanglORCiD, Jan HoffmannORCiDGND, Alicia Just, Nina MorgnerORCiDGND |
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URN: | urn:nbn:de:hebis:30:3-695204 |
DOI: | https://doi.org/10.1038/s41467-022-28828-1 |
ISSN: | 2041-1723 |
Parent Title (English): | Nature Communications |
Publisher: | Nature Publishing Group UK |
Place of publication: | [London] |
Document Type: | Article |
Language: | English |
Date of Publication (online): | 2022/03/08 |
Date of first Publication: | 2022/03/08 |
Publishing Institution: | Universitätsbibliothek Johann Christian Senckenberg |
Release Date: | 2023/07/27 |
Tag: | Membrane proteins Bioenergetics; Mass spectrometry |
Volume: | 13 |
Issue: | art. 1218 |
Article Number: | 1218 |
Page Number: | 13 |
First Page: | 1 |
Last Page: | 13 |
Note: | Open Access funding enabled and organized by Projekt DEAL. |
Note: | The data generated in this study have been deposited in the Zenodo database and are available at https://doi.org/10.5281/zenodo.5865003 |
HeBIS-PPN: | 511236727 |
Institutes: | Biochemie, Chemie und Pharmazie |
Dewey Decimal Classification: | 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie |
Sammlungen: | Universitätspublikationen |
Licence (German): | Creative Commons - CC BY - Namensnennung 4.0 International |