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Titolo:
His(15) of subunit a of the Escherichia coli ATP synthase is important forthe structure or assembly of the membrane sector F-o
Autore:
Patterson, AR; Wada, T; Vik, SB;
Indirizzi:
So Methodist Univ, Dept Biol Sci, Dallas, TX 75275 USA So Methodist Univ Dallas TX USA 75275 Dept Biol Sci, Dallas, TX 75275 USA
Titolo Testata:
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
fascicolo: 1, volume: 368, anno: 1999,
pagine: 193 - 197
SICI:
0003-9861(19990801)368:1<193:HOSAOT>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
F-0 SECTOR; B-SUBUNIT; NUCLEOTIDE-SEQUENCE; ALPHA-SUBUNIT; UNC OPERON; INSERTION; TRANSLOCATION; MUTAGENESIS; TOPOLOGY; RESIDUES;
Keywords:
ATP synthase; mutagenesis; proton translocation; subunit a; F-o;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Vik, SB So Methodist Univ, Dept Biol Sci, Dallas, TX 75275 USA So Methodist Univ Dallas TX USA 75275 l Sci, Dallas, TX 75275 USA
Citazione:
A.R. Patterson et al., "His(15) of subunit a of the Escherichia coli ATP synthase is important forthe structure or assembly of the membrane sector F-o", ARCH BIOCH, 368(1), 1999, pp. 193-197

Abstract

Approximately 37 amino acids at the amino-terminus of subunit a of the Escherichia coli ATP synthase are found localized to the periplasm. Results indicate that a single amino acid substitution, H15D, disrupts assembly of subunit a and causes a loss of ATP synthase function. In this study, a conserved region of nine amino acids, 11-19, was initially mutagenized randomly, generating no mutants that could grow on succinate-minimal medium, Subsequent mutagenesis, confined to residues His(14), His(15), and Asn(17), indicated that constructs containing H15D were the most deleterious, Four single mutants were constructed and analyzed: H15A, H14D, H15A, and H15D. Only H15Dwas significantly impaired, with respect to ATP-driven proton translocation, passive proton permeability through F-o, and sensitivity of membrane-bound ATPase to DCCD. Immunoblot analysis indicated very low levels of subunita from H15D, Cysteine mutations were constructed at positions 14, 15, 17, and 18. Residues 14, 15, and 17 were shown to be accessible in the periplasmic space, while residue 18 was not, indicating that this region was stablyfolded. While both His(14) and His(15) are conserved among a group of bacteria, results presented here indicate that they are not equivalent, and that a specific role for His'S in the assembly or structure of the ATP synthase is supported. (C) 1999 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 02:53:13