This preprint is under consideration at a Nature Portfolio Journal. A preprint is a preliminary version of a manuscript that has not completed peer review at a journal. Research Square does not conduct peer review prior to posting preprints. The posting of a preprint on this server should not be interpreted as an endorsement of its validity or suitability for dissemination as established information or for guiding clinical practice.
Nature journals have partnered with Research Square to offer In Review, a journal-integrated preprint deposition service.
Article
Nina Morgner
Goethe University Frankfurt
Corresponding Author
ORCiD: https://orcid.org/0000-0002-1872-490X
License:
This work is licensed under a CC BY 4.0 License. Read Full License
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 of 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.
Keywords
F-type ATP synthases, multiprotein complexes, functional F1 complex.
Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
Figure 6
Figure 7
Figure 8
Figure 9
Figure 10
There is NO Competing Interest.
This is a list of supplementary files associated with this preprint. Click to download.
Loading...
Badges
Prescreen
This manuscript passed our Prescreen assessment
Complete author information
Appropriate declaration statements
Potential risks to human health
Prescreen
Peer Review Timeline
CURRENT STATUS: Under Review
Version 1
Posted 20 Jan, 2021
Metrics
Comments: 0
PDF Downloads: ...
HTML Views: ...
Learn more about our company.
This preprint is under consideration at a Nature Portfolio Journal. A preprint is a preliminary version of a manuscript that has not completed peer review at a journal. Research Square does not conduct peer review prior to posting preprints. The posting of a preprint on this server should not be interpreted as an endorsement of its validity or suitability for dissemination as established information or for guiding clinical practice.
Nature journals have partnered with Research Square to offer In Review, a journal-integrated preprint deposition service.
Article
Nina Morgner
Goethe University Frankfurt
Corresponding Author
ORCiD: https://orcid.org/0000-0002-1872-490X
Badges
Prescreen
This manuscript passed our Prescreen assessment
Complete author information
Appropriate declaration statements
Potential risks to human health
Prescreen
Peer Review Timeline
CURRENT STATUS: Under Review
Version 1
Posted 20 Jan, 2021
Metrics
Comments: 0
PDF Downloads: ...
HTML Views: ...
License:
This work is licensed under a CC BY 4.0 License. Read Full License
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 of 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.
Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
Figure 6
Figure 7
Figure 8
Figure 9
Figure 10
There is NO Competing Interest.
This is a list of supplementary files associated with this preprint. Click to download.
Loading...