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Titolo:
EFFECTS OF CARBON SOURCE ON EXPRESSION OF F-0 GENES AND ON THE STOICHIOMETRY OF THE C-SUBUNIT IN THE F1F0 ATPASE OF ESCHERICHIA-COLI
Autore:
SCHEMIDT RA; QU J; WILLIAMS JR; BRUSILOW WSA;
Indirizzi:
WAYNE STATE UNIV,SCH MED,DEPT BIOCHEM & MOL BIOL,SCOTT HALL,540 E CANFIELD AVE DETROIT MI 48201 WAYNE STATE UNIV,SCH MED,DEPT BIOCHEM & MOL BIOL DETROIT MI 48201
Titolo Testata:
Journal of bacteriology
fascicolo: 12, volume: 180, anno: 1998,
pagine: 3205 - 3208
SICI:
0021-9193(1998)180:12<3205:EOCSOE>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
DICYCLOHEXYLCARBODIIMIDE-BINDING PROTEIN; H+-ATPASE; SITE MUTATION; UNC OPERON; COMPLEX; IDENTIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
19
Recensione:
Indirizzi per estratti:
Citazione:
R.A. Schemidt et al., "EFFECTS OF CARBON SOURCE ON EXPRESSION OF F-0 GENES AND ON THE STOICHIOMETRY OF THE C-SUBUNIT IN THE F1F0 ATPASE OF ESCHERICHIA-COLI", Journal of bacteriology, 180(12), 1998, pp. 3205-3208

Abstract

Expression of the genes for the membrane-bound F-0 sector of the Escherichia coli F1F0 proton-translocating ATPase can respond to changes in metabolic conditions, and these changes are reflected in alterationsin the subunit stoichiometry of the oligomeric F-0 proton channel, Transcriptional and translational lacZ fusions to the promoter and to two F-0 genes show that, during growth on the nonfermentable carbon source succinate, transcription of the operon and translation of uncB, encoding the a subunit of F-0, are higher than during growth on glucose. In contrast, translation of the uncE gene, encoding the c subunit of F-0, is higher during growth on glucose than during growth on succinate, Translation rates of both uncB and uncE change as culture density increases, but transcription rates do not. Quantitation of the c stoichiometry shows that more c subunits are assembled into the F1F0 ATPase in cells grown on glucose than in cells grown on succinate, E. coli therefore appears to have a mechanism for regulating the composition and,presumably, the function of the ATPase in response to metabolic circumstances.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 20:44:24