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Yeast mitochondrial F 1 F 0 ‐ATPase: the novel subunit e is identical to Tim11
Author(s) -
Arnold Isabel,
Bauer Matthias F.,
Brunner Michael,
Neupert Walter,
Stuart Rosemary A.
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00691-1
Subject(s) - protein subunit , atpase , gamma aminobutyric acid receptor subunit alpha 1 , saccharomyces cerevisiae , biology , inner mitochondrial membrane , mitochondrion , biochemistry , specificity factor , v atpase , yeast , microbiology and biotechnology , enzyme , g alpha subunit , gene , gene expression , promoter
We report here the identification of the novel subunit of the mitochondrial F 1 F 0 ‐ATPase from Saccharomyces cerevisiae , ATPase subunit e. Yeast ATPase subunit e displays significant similarities in both amino acid sequence, properties (hydropathy and predicted coiled‐coil structure) and orientation in the inner membrane, with previously identified mammalian ATPase subunit e proteins. Estimation of its native molecular mass and ability to be co‐immunoprecipitated with α subunit of the F 1 ‐ATPase, demonstrate that subunit e is a subunit of the F 1 F 0 ‐ATPase. Stable expression of subunit e requires the presence of the mitochondrially encoded subunits of the F 0 ‐ATPase. Subunit e had been previously identified as Tim11 and was proposed to be involved in the process of sorting of proteins to the mitochondrial inner membrane.