TY  - JOUR
A1  - Arnold, Isabel
A1  - Pfeiffer, Kathy
A1  - Neupert, Walter
A1  - Stuart, Rosemary A.
A1  - Schägger, Hermann
T1  - ATP synthase of yeast mitochondria : isolation of subunit j and disruption of the ATP18 gene
T2  - Journal of biological chemistry
N2  - The subunit composition of the mitochondrial ATP synthase from Saccharomyces cerevisiae was analyzed using blue native gel electrophoresis and high resolution SDS-polyacrylamide gel electrophoresis. We report here the identification of a novel subunit of molecular mass of 6,687 Da, termed subunit j (Su j). An open reading frame of 127 base pairs (ATP18), which encodes for Su j, was identified on chromosome XIII. Su j does not display sequence similarity to ATP synthase subunits from other organisms. Data base searches, however, identified a potential homolog from Schizosaccharomyces pombe with 51% identity to Su j of S. cerevisiae. Su j, a small protein of 59 amino acid residues, has the characteristics of an integral inner membrane protein with a single transmembrane segment. Deletion of the ATP18 gene encoding Su j led to a strain (Deltasu j) completely deficient in oligomycin-sensitive ATPase activity and unable to grow on nonfermentable carbon sources. The presence of Su j is required for the stable expression of subunits 6 and f of the F0 membrane sector. In the absence of Su j, spontaneously arising rho- cells were observed that lacked also ubiquinol-cytochrome c reductase and cytochrome c oxidase activities. We conclude that Su j is a novel and essential subunit of yeast ATP synthase.
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/75861
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-758613
SN  - 0021-9258
VL  - 274.1999
IS  - 1
SP  - 36
EP  - 40
PB  - American Society for Biochemistry and Molecular Biology Publications
CY  - Bethesda, Md
ER  -