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Titolo:
AN NA-PUMPING V1V0-ATPASE COMPLEX IN THE THERMOPHILIC BACTERIUM CLOSTRIDIUM-FERVIDUS()
Autore:
BENTRUP KHZ; UBBINKKOK T; LOLKEMA JS; KONINGS WN;
Indirizzi:
UNIV GRONINGEN,CTR BIOL,DEPT MICROBIOL,KERKLAAN 30 NL-9751 NN HAREN NETHERLANDS UNIV GRONINGEN,GRONINGEN BIOMOL SCI & BIOTECHNOL INST,DEPT MICROBIOL NL-9751 NN HAREN NETHERLANDS
Titolo Testata:
Journal of bacteriology
fascicolo: 4, volume: 179, anno: 1997,
pagine: 1274 - 1279
SICI:
0021-9193(1997)179:4<1274:ANVCIT>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
VACUOLAR H+-ATPASE; V-TYPE ATPASE; TRANSLOCATING ATPASE; THERMUS-THERMOPHILUS; ENTEROCOCCUS-HIRAE; ESCHERICHIA-COLI; UNC OPERON; ACETOBACTERIUM-WOODII; NUCLEOTIDE-SEQUENCE; MOLECULAR-CLONING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
33
Recensione:
Indirizzi per estratti:
Citazione:
K.H.Z. Bentrup et al., "AN NA-PUMPING V1V0-ATPASE COMPLEX IN THE THERMOPHILIC BACTERIUM CLOSTRIDIUM-FERVIDUS()", Journal of bacteriology, 179(4), 1997, pp. 1274-1279

Abstract

Energy transduction in the anaerobic, thermophilic bacterium Clostridium fervidus relies exclusively on Na+ as the coupling ion. The Na+ ion gradient across the membrane is generated by a membrane-hound ATPase(G, Speelmans, B, Poolman, T, Abee, and W. N, Konings, J, Bacteriol, 176:5160-5162, 1994), The Na+-ATPase complex was purified to homogeneity. It migrates as a single band in native polyacrylamide gel electrophoresis and catalyzes Na+-stimulated ATPase activity. Denaturing gel electrophoresis shelved that the complex consists of at least six different polypeptides with apparent molecular sizes of 66, 61, 51, 37, 26,and 17 kDa. The N-terminal sequences of the 66- and 51-kDa subunits were found to be significantly homologous to subunits A and B, respectively, of the Na+-translocating V-type ATPase of Enterococcus hirae. The purified V1V0 protein complex was reconstituted in a mixture of Escherichia coil phosphatidylethanolamine and egg yolk phosphatidylcholineand shown to catalyze the uptake of Na+ ions upon hydrolysis of ATP. Na+ transport was completely abolished by monensin, whereas valinomycin stimulated the uptake rate, This is indicative of electrogenic sodium transport, The presence of the protonophore SF6847 had no significant effect on the uptake, indicating that Na+ translocation is a primaryevent and in the cell is not accomplished by an H+-translocating pumpin combination with an Na+-H+ antiporter.

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Documento generato il 30/09/20 alle ore 05:21:29