Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
THE A(LEU207)-]ARG MUTATION IN F(1)F(0)-ATP SYNTHASE FROM ESCHERICHIA-COLI - A MODEL FOR HUMAN MITOCHONDRIAL DISEASE
Autore:
HARTZOG PE; CAIN BD;
Indirizzi:
UNIV FLORIDA,DEPT BIOCHEM & MOLEC BIOL,BOX 100245 JHMHC GAINESVILLE FL 32610 UNIV FLORIDA,DEPT BIOCHEM & MOLEC BIOL,BOX 100245 JHMHC GAINESVILLE FL 32610
Titolo Testata:
The Journal of biological chemistry
fascicolo: 17, volume: 268, anno: 1993,
pagine: 2250 - 2252
SICI:
0021-9258(1993)268:17<2250:TAMIFS>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTON-TRANSLOCATING ATPASE; ALPHA-SUBUNIT; H+-ATPASE; A-SUBUNIT; NUCLEOTIDE-SEQUENCE; F1F0-ATP SYNTHASE; UNC OPERON; PORE; F0F1-ATPASE; REGION;
Tipo documento:
Note
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
P.E. Hartzog e B.D. Cain, "THE A(LEU207)-]ARG MUTATION IN F(1)F(0)-ATP SYNTHASE FROM ESCHERICHIA-COLI - A MODEL FOR HUMAN MITOCHONDRIAL DISEASE", The Journal of biological chemistry, 268(17), 1993, pp. 2250-2252

Abstract

The mitochondrial ATPase 6 gene encodes a subunit of F1F0 adenosine triphosphate (ATP) synthase. A mutation in the ATPase 6 gene has been genetically linked to two maternally inherited genetic diseases: neurological muscle weakness, ataxia, and retinitis pigmentosa (NARP) and certain cases of subacute necrotizing encephalopathy (SNE). Although theseverity of both NARP and SNE disease were correlated with the quantity of the ATPase 6leu156-->arg mutation in each patient, the mutation could not be shown to alter F1F0-ATP synthase activity. To investigatethe biochemical effects of the ATPase 6leu156-->arg mutation on F1F0-ATP synthase, the a(leu207-->arg) mutation was constructed in the F1F0-ATP synthase from Escherichia coli to serve as a model for the disease mutation. Characterization of the model bacterial enzyme revealed that the mutation abolishes detectable ATP synthesis via oxidative phosphorylation. The a(leu207-->arg) mutation results in a structural perturbation blocking proton translocation through F1F0-ATP synthase. The results suggest that a structural defect in human F1F0-ATP synthase is the biochemical basis for NARP and SNE.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/09/20 alle ore 05:41:26