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Titolo:
INTERACTION OF THE DELTA-SUBUNIT AND B-SUBUNIT CONTRIBUTES TO F1 AND F-0 INTERACTION IN THE ESCHERICHIA-COLI F1F0-ATPASE
Autore:
SAWADA K; KURODA N; WATANABE H; MORITANIOTSUKA C; KANAZAWA H;
Indirizzi:
OKAYAMA UNIV,FAC ENGN,DEPT BIOTECHNOL OKAYAMA 700 JAPAN OKAYAMA UNIV,FAC ENGN,DEPT BIOTECHNOL OKAYAMA 700 JAPAN
Titolo Testata:
The Journal of biological chemistry
fascicolo: 48, volume: 272, anno: 1997,
pagine: 30047 - 30053
SICI:
0021-9258(1997)272:48<30047:IOTDAB>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTON-TRANSLOCATING ATPASE; H+-ATPASE; EPSILON-SUBUNIT; NUCLEOTIDE-SEQUENCE; ALPHA-SUBUNIT; ADENOSINE-TRIPHOSPHATASE; COUPLING FACTOR; GAMMA-SUBUNIT; BETA-SUBUNIT; UNC OPERON;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
55
Recensione:
Indirizzi per estratti:
Citazione:
K. Sawada et al., "INTERACTION OF THE DELTA-SUBUNIT AND B-SUBUNIT CONTRIBUTES TO F1 AND F-0 INTERACTION IN THE ESCHERICHIA-COLI F1F0-ATPASE", The Journal of biological chemistry, 272(48), 1997, pp. 30047-30053

Abstract

Interactions of the F-1-F-0-ATPase subunits between the cytoplasmic domain of the b subunit (residues 26-156, b(cyt)) and other membrane peripheral subunits including alpha, beta, gamma, delta, epsilon, and putative cytoplasmic domains of the a subunit were analyzed with the yeast two-hybrid system and in vitro reconstitution of ATPase from the purified subunits as well, Only the combination of b(cyt) fused to the activation domain of the yeast GAL-4, and delta subunit fused to the DNA binding domain resulted in the strong expression of the beta-galactosidase reporter gene, suggesting a specific interaction of these subunits, Expression of b(cyt) fused to glutathione S-transferase (GST) together with the delta subunit in Escherichia coil resulted in the overproduction of these subunits in soluble form, whereas expression of theGST-b(cyt) fusion alone had no such effect, indicating that GST-b(cyt) was protected by the co-expressed delta subunit from proteolytic attack in the cell, These results indicated that the membrane peripheral domain of b subunit stably interacted with the delta subunit in the cell, The affinity purified GST-b(cyt) did not contain significant amounts of delta, suggesting that the interaction of these subunits was relatively weak, Binding of these subunits observed in a direct binding assay significantly supported the capability of binding of the subunits, The ATPase activity was reconstituted from the purified b(cyt) together with alpha, beta, gamma, delta, and epsilon, or with the same combination except epsilon, Specific elution of the ATPase activity from glutathione affinity column with the addition of glutathione after reconstitution demonstrated that the reconstituted ATPase formed a complex, The result indicated that interaction of b and delta was stabilized by F-1 subunits other than epsilon and also suggested that b-delta interaction was important for F-1-F-0 interaction.

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Documento generato il 30/09/20 alle ore 05:12:14