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PMID: 17350625 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Metabolism controls dimerization of the chloroplast FoF1 ATP synthase in Chlamydomonas reinhardtii.

FEBS letters ·Vol. 581 ·No. 7 ·2007-04-03 ·Pages 1391-6

Schwassmann HJ, Rexroth S, Seelert H, Dencher NA

Abstract

Dimers and oligomers of F-type ATP synthases have been observed previously in mitochondria of various organisms and for the CF(o)F(1) ATP synthase of chloroplasts of Chlamydomonas reinhardtii. In contrast to mitochondria, however, dimers of chloroplast ATP synthases dissociate at elevated phosphate concentration. This suggests a regulation by cell physiological processes. Stable isotope labeling of living cells and blue-native PAGE have been employed to quantitate changes in the ratio of monomeric to dimeric CF(o)F(1) ATP synthase. Chlamydomonas reinhardtii cells were cultivated photoautotrophically in the presence of (15)N and photomixotrophically at natural (14)N abundance, respectively. As compared to photoautotrophic growth, an increased assembly of ATP synthase dimers on the expense of preexisting monomers during photomixotrophic growth was observed, demonstrating a metabolic control of the dimerization process.

MeSH Terms
Animals Chlamydomonas reinhardtii/enzymology Chloroplasts/enzymology Dimerization Electrophoresis, Polyacrylamide Gel Isotope Labeling Proton-Translocating ATPases/chemistry,metabolism Protozoan Proteins/chemistry,metabolism
Chemicals
Protozoan Proteins Proton-Translocating ATPases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Schwassmann Helena J
Physical Biochemistry, Department of Chemistry, Darmstadt University of Technology, Petersenstrasse 22, D-64287 Darmstadt, Germany. [email protected]
Rexroth Sascha
Seelert Holger
Dencher Norbert A
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
2007-04-03
Epub
2007-00-02
Pages
1391-6
Language
English
Region
England
NLM ID
0155157
Subset
IM
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