| Chapter title |
Purification and Reconstitution of Ilyobacter tartaricus ATP Synthase
|
|---|---|
| Chapter number | 3 |
| Book title |
Molecular Motors
|
| Published in |
Methods in molecular biology, January 2018
|
| DOI | 10.1007/978-1-4939-8556-2_3 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-8554-8, 978-1-4939-8556-2
|
| Authors |
Ganna O. Krasnoselska, Thomas Meier |
| Abstract |
F-type adenosine triphosphate (ATP) synthase is a membrane-bound macromolecular complex, which is responsible for the synthesis of ATP, the universal energy source in living cells. This enzyme uses the proton- or sodium-motive force to power ATP synthesis by a unique rotary mechanism and can also operate in reverse, ATP hydrolysis, to generate ion gradients across membranes. The F1Fo-ATP synthases from bacteria consist of eight different structural subunits, forming a complex of ∼550 kDa in size. In the bacterium Ilyobacter tartaricus the ATP synthase has the stoichiometry α3β3γδεab2c11. This chapter describes a wet-lab working protocol for the purification of several tens of milligrams of pure, heterologously (E. coli-)produced I. tartaricus Na+-driven F1Fo-ATP synthase and its subsequent efficient reconstitution into proteoliposomes. The methods are useful for a broad range of subsequent biochemical and biotechnological applications. |
Mendeley readers
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 8 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Bachelor | 2 | 25% |
| Other | 1 | 13% |
| Student > Ph. D. Student | 1 | 13% |
| Student > Master | 1 | 13% |
| Professor > Associate Professor | 1 | 13% |
| Other | 1 | 13% |
| Unknown | 1 | 13% |
| Readers by discipline | Count | As % |
|---|---|---|
| Biochemistry, Genetics and Molecular Biology | 4 | 50% |
| Agricultural and Biological Sciences | 2 | 25% |
| Nursing and Health Professions | 1 | 13% |
| Physics and Astronomy | 1 | 13% |