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Titolo:
ON THE ROLE OF ARG-210 AND GLU-219 OF SUBUNIT-ALPHA IN PROTON TRANSLOCATION BY THE ESCHERICHIA-COLI F0F1-ATP SYNTHASE
Autore:
VALIYAVEETIL FI; FILLINGAME RH;
Indirizzi:
UNIV WISCONSIN,SCH MED,DEPT BIOMOL CHEM,587 MED SCI BLDG MADISON WI 53706 UNIV WISCONSIN,SCH MED,DEPT BIOMOL CHEM MADISON WI 53706
Titolo Testata:
The Journal of biological chemistry
fascicolo: 51, volume: 272, anno: 1997,
pagine: 32635 - 32641
SICI:
0021-9258(1997)272:51<32635:OTROAA>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
F1F0 ATP SYNTHASE; POLAR LOOP REGION; H+-ATPASE; A-SUBUNIT; SUPPRESSOR MUTATIONS; NUCLEOTIDE-SEQUENCE; MUTAGENIC ANALYSIS; UNC OPERON; F-0; BINDING;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
41
Recensione:
Indirizzi per estratti:
Citazione:
F.I. Valiyaveetil e R.H. Fillingame, "ON THE ROLE OF ARG-210 AND GLU-219 OF SUBUNIT-ALPHA IN PROTON TRANSLOCATION BY THE ESCHERICHIA-COLI F0F1-ATP SYNTHASE", The Journal of biological chemistry, 272(51), 1997, pp. 32635-32641

Abstract

A strain of Escherichia coli was constructed which had a complete deletion of the chromosomal uncB gene encoding subunit alpha of the F0F1-ATP synthase, Gene replacement was facilitated by a selection protocolthat utilized the sacB gene of Bacillus subtilis cloned in a kanamycin resistance cartridge (Ried, J. L., and Collmer, A. (1987) Gene (Amst.) 57, 239-246). F-0 subunits b and c inserted normally into the membrane in the Delta uncB strain. This observation confirms a previous report (Hermolin, J., and Fillingame, R. H. (1995) J. Biol. Chem, 270, 2815-2817) that subunit alpha is not required for the insertion of subunits b and c, The Delta uncB strain has been used to characterize mutations in Arg-210 and Glu-219 of subunit alpha, residues previously postulated to be essential in proton translocation, The alpha E219G and alpha E219K mutants grew on a succinate carbon source via oxidative phosphorylation and membranes from these mutants exhibited ATPase-coupled proton translocation (i.e. ATP driven 9-amino-6-chloromethoxyacridine quenching responses that were 60-80% of wild type membranes), We conclude that the alpha Glu-219 residue cannot play a critical role in proton translocation. The alpha R210A mutant did not grow on succinate andmembranes exhibited no ATPase-coupled proton translocation, However, on removal of F-1 from membrane, the alpha R210A mutant F-0 was activein passive proton translocation, i.e. in dissipating the Delta pH normally established by NADH oxidation with these membrane vesicles. alpha R210A membranes with F-1 bound were also proton permeable. Arg-210 of subunit a may play a critical role in active H+ transport that is coupled to ATP synthesis or hydrolysis, but is not essential for the translocation of protons across the membranes.

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Documento generato il 30/09/20 alle ore 05:00:37