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Titolo:
Hybrid Rhodospirillum rubrum F0F1 ATP synthases containing spinach chloroplast F-1 beta or alpha and beta subunits reveal the essential role of the alpha subunit in ATP synthesis and tentoxin sensitivity
Autore:
Tucker, WC; Du, ZY; Hein, R; Richter, ML; Gromet-Elhanan, Z;
Indirizzi:
Weizmann Inst Sci, Dept Biol Chem, IL-76100 Rehovot, Israel Weizmann Inst Sci Rehovot Israel IL-76100 Chem, IL-76100 Rehovot, Israel Univ Kansas, Dept Mol Biosci, Lawrence, KS 66045 USA Univ Kansas LawrenceKS USA 66045 Dept Mol Biosci, Lawrence, KS 66045 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 2, volume: 275, anno: 2000,
pagine: 906 - 912
SICI:
0021-9258(20000114)275:2<906:HRRFAS>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
F1 ADENOSINE-TRIPHOSPHATASE; ESCHERICHIA-COLI F1-ATPASE; CROSS-LINKING; DELTA-SUBUNITS; 2ND STALK; ROTATION; COMPLEX; BINDING; RECONSTITUTION; PURIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
51
Recensione:
Indirizzi per estratti:
Indirizzo: Gromet-Elhanan, Z Weizmann Inst Sci, Dept Biol Chem, IL-76100 Rehovot, Israel Weizmann Inst Sci Rehovot Israel IL-76100 ovot, Israel
Citazione:
W.C. Tucker et al., "Hybrid Rhodospirillum rubrum F0F1 ATP synthases containing spinach chloroplast F-1 beta or alpha and beta subunits reveal the essential role of the alpha subunit in ATP synthesis and tentoxin sensitivity", J BIOL CHEM, 275(2), 2000, pp. 906-912

Abstract

Trace amounts (similar to 55%) of the chloroplast or subunit were found tobe absolutely required for effective restoration of catalytic function to LiCl-treated chromatophores of Rhodospirillum rubrum with the chloroplast beta subunit (Avital, S., and Gromet-Elhanan, Z. (1991) J. Biol. Chem. 266, 7067-7072). To clarify the role of the Lu subunit in the rebinding of beta,restoration of catalytic function, and conferral of sensitivity to the chloroplast-specific inhibitor tentoxin, LiCl-treated chromatophores were analyzed by immunoblotting before and after reconstitution with mixtures of R. rubrum and chloroplast alpha and beta subunits. The treated chromatophores were found to have lost, in addition to most of their beta subunits, approximately a third of the alpha subunits, and restoration of catalytic activity required rebinding of both subunits. The hybrid reconstituted with the R.rubrum alpha and chloroplast beta subunits was active in ATP synthesis as well as hydrolysis, and both activities were completely resistant to tentoxin. In contrast, a hybrid reconstituted with both chloroplast or and beta subunits restored only a MgATPase activity, which was fully inhibited by tentoxin, These results indicate that all three copies of the R. rubrum alpha subunit are required for proton-coupled ATP synthesis, whereas for conferral of tentoxin sensitivity at least one copy of the chloroplast alpha subunit is required together with the chloroplast beta subunit. The hybrid systemwas further used to examine the effects of amino acid substitution at position 83 of the beta subunit on sensitivity to tentoxin.

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Documento generato il 01/10/20 alle ore 16:11:17