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Titolo:
Site-directed mutations in the mitochondrially encoded subunits I and III of yeast cytochrome oxidase
Autore:
Meunier, B;
Indirizzi:
Univ Coll London, Dept Biol, London WC1E 6BT, England Univ Coll London London England WC1E 6BT Biol, London WC1E 6BT, England
Titolo Testata:
BIOCHEMICAL JOURNAL
, volume: 354, anno: 2001,
parte:, 2
pagine: 407 - 412
SICI:
0264-6021(20010301)354:<407:SMITME>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
C-OXIDASE; RHODOBACTER-SPHAEROIDES; PROTON-TRANSFER; SACCHAROMYCES-CEREVISIAE; SIDEROBLASTIC ANEMIA; POINT MUTATIONS; WILD-TYPE; MUTANTS; PROTEINS; ANGSTROM;
Keywords:
cytochrome c oxidase; disease-associated mutations; Saccharomyces cerevisiae;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Meunier, B Univ Coll London, Dept Biol, Gower St, London WC1E 6BT, EnglandUniv Coll London Gower St London England WC1E 6BT 6BT, England
Citazione:
B. Meunier, "Site-directed mutations in the mitochondrially encoded subunits I and III of yeast cytochrome oxidase", BIOCHEM J, 354, 2001, pp. 407-412

Abstract

Since yeast is amenable to mitochondrial transformation, designed mutations can be introduced in the mitochondrially encoded subunits of the respiratory complexes. In the present work, six mutations have been introduced by the biolistic method into yeast (Saccharomyces cerevisiae) cytochrome oxidase subunits I and III. The effects of these mutations on respiratory growth competence, cytochrome oxidase activity and optical properties were then characterized. Firstly, the conserved glutamate Glu-243 in the D-channel of subunit I was replaced by an asparagine or an aspartate residue. The effectsof the mutations showed that Glu-243, which is essential for proton movement in bacterial oxidases, is also required for the activity of the eukaryotic enzyme. Secondly, four mutations associated with human disease were introduced in yeast, allowing detailed analysis of their deleterious effects oncytochrome oxidase function: Met-273-->Thr, Ile-280-->Thr and Gly-317-->Ser, affecting residues located in or near the K-channel in subunit I, and a short in-frame deletion comprising residues Phe-102 to Phe-106 in subunit III (Delta F102-F106). The subunit III mutation was highly deleterious and abolished enzyme assembly. The change GIy-317 -->Ser had no effect on respiratory function. However, mutations Met-273-->Thr and IIe-280-->Thr were mildly deleterious, decreased cytochrome oxidase activity and slightly perturbed the properties of the binuclear centre.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/01/20 alle ore 14:55:19