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| THE ROLE OF THE STALK IN THE COUPLING MECHANISM OF F1F0-ATPASES |
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| Author(s): WALKER JE, COLLINSON IR |
| Source: FEBS LETTERS Volume: 346 Issue: 1 Pages: 39-43 Published: JUN 6 1994 |
| Times Cited: 58 References: 43 |
| Abstract: The extrinsic and intrinsic membrane sectors of F1F0-ATPases are linked by a slender stalk 40-50 Angstrom in length. The stalk transmits the energy produced by oxidative or photosynthetic phosphorylation from the intrinsic sector, F-0, to the catalytic sites in the extrinsic F-1 sector. How this is achieved is unknown, but long-range conformational changes linked to transmembrane proton transport may be involved. In bacterial and chloroplast F1F0-ATPases, the stalk is probably a composite of subunits delta and epsilon, part of the gamma-subunit, and the extrinsic membrane domains of 2 subunits (identical or non-identical according to the species) that are bound to the membrane by their N-terminal regions. The stalk in the bovine mitochondrial enzyme appears to be more complex, and the gamma, delta, epsilon, OSCP, F-6, b and d subunits all contribute to it. A bovine stalk complex has been assembled in vitro from bacterially expressed OSCP, F-6, b and d, both in the presence and in the absence of F-1-ATPase. One molecule of each of these subunits is present in the assembled complexes, as there is also in each native F1F0-ATPase assembly. Providing that suitable crystals can be obtained, the stalk complex and the F-1 stalk complex may permit the high resolution structure of bovine F-1-ATPase to be extended into the stalk domain. Abstract |
| Document Type: Proceedings Paper |
| Language: English |
| Reprint Address: WALKER, JE (reprint author), MRC, MOLEC BIOL LAB, HILLS RD, CAMBRIDGE CB2 2QH, ENGLAND |
| Publisher: ELSEVIER SCIENCE BV, PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS |
| Subject Category: Biochemistry & Molecular Biology; Biophysics; Cell Biology |
| IDS Number: NQ569 |
| ISSN: 0014-5793 |
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