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Titolo:
A MUTATION IN WHICH ALANINE-128 IS REPLACED BY ASPARTIC-ACID ABOLISHES DIMERIZATION OF THE B-SUBUNIT OF THE F0F1-ATPASE FROM ESCHERICHIA-COLI
Autore:
HOWITT SM; RODGERS AJW; JEFFREY PD; COX GB;
Indirizzi:
AUSTRALIAN NATL UNIV,JOHN CURTIN SCH MED RES,DIV BIOCHEM & MOLEC BIOL,GPO BOX 334 CANBERRA ACT 2601 AUSTRALIA
Titolo Testata:
The Journal of biological chemistry
fascicolo: 12, volume: 271, anno: 1996,
pagine: 7038 - 7042
SICI:
0021-9258(1996)271:12<7038:AMIWAI>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTON-TRANSLOCATING ATPASE; ADENOSINE-TRIPHOSPHATASE; NUCLEOTIDE-SEQUENCE; UNC OPERON; C-SUBUNIT; SYNTHASE; PERMEABILITY; ORGANIZATION; PORTION; GENES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
29
Recensione:
Indirizzi per estratti:
Citazione:
S.M. Howitt et al., "A MUTATION IN WHICH ALANINE-128 IS REPLACED BY ASPARTIC-ACID ABOLISHES DIMERIZATION OF THE B-SUBUNIT OF THE F0F1-ATPASE FROM ESCHERICHIA-COLI", The Journal of biological chemistry, 271(12), 1996, pp. 7038-7042

Abstract

Site-directed mutagenesis was used to investigate the roles of a short, series of hydrophobic amino acids in the b-subunit of the Escherichia coli F0F1-ATPase. A mutation affecting one of these, G131D, had been previously characterized and was found to interrupt assembly of the F0F1-ATPase (Jans, D. A., Hatch, L., Fimmel, A. L., Gibson, D., and Cox, G. B. (1985) J. Bacteriol. 162, 420-426). To extend this work, aspartic acid was substituted for each one of the residues from positions 124 to 132. The properties of mutants in this series are consistent with the region hom Val(124) to Gly(131) forming an alpha-helix. Two of the mutations, V124D and A128D, resulted in a similar phenotype to theG131D mutation. This suggested that Val(124), Ala(128), and Gly(131) form a helical face which may have a role in inter- or intrasubunit interactions, This was tested by overexpressing and purifying the cytoplasmic domains of the wild type and A128D mutant b-subunits. Sedimentation equilibrium centrifugation indicated that the wild type domain formed a dimer whereas the mutant was present as a monomer.

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Documento generato il 30/09/20 alle ore 05:45:31