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Fourteen protomers compose the oligomer III of the proton-rotor in spinach chloroplast ATP synthase.

Abstract：

:Three fundamentally different chloroplast ATP synthase samples of increasing complexity were visualized by atomic force microscopy. The samples are distinguishable in respect to the isolation technique, the detergent employed, and the final subunit composition. The homo-oligomer III was isolated following SDS treatment of ATP synthase, the proton-turbine III+IV was obtained by blue-native electrophoresis, and complete CFO was isolated by anion exchange chromatography of NaSCN splitted ATP synthase. In all three ATP synthase subcomplexes 14 and only 14 circularly arranged subunits III composed the intact transmembrane rotor. Therefore, 14 protomers built the membrane-resident proton turbine. The observed stoichiometry of 14 is not a biochemical artifact or affected by natural growth variations of the spinach, as previously suggested. A correlation between the presence of subunit IV in the imaged sample and the appearance of a central protrusion in the narrower orifice of the oligomeric cylinder III14 has been observed. In contrast to current predictions, in chloroplast FO the subunit IV can be found inside the cylinder III14 and not at its periphery, at least in the reconstituted 2D arrays imaged.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Seelert H,Dencher NA,Müller DJ

doi

10.1016/j.jmb.2003.08.046

keywords:

subject

Has Abstract

pub_date

2003-10-17 00:00:00

pages

337-44

issue

2

eissn

0022-2836

issn

1089-8638

pii

S002228360301088X

journal_volume

333

pub_type

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