Premium
Turnover of ATP synthase subunits in F 1 ‐depleted HeLa and yeast cells
Author(s) -
Rak Malgorzata,
McStay Gavin P.,
Fujikawa Makoto,
Yoshida Masasuke,
Manfredi Giovanni,
Tzagoloff Alexander
Publication year - 2011
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/j.febslet.2011.07.011
Subject(s) - protein subunit , atp synthase , v atpase , mitochondrion , atp synthase gamma subunit , hela , yeast , saccharomyces cerevisiae , atpase , biology , biochemistry , mitochondrial matrix , inner mitochondrial membrane , f atpase , cytosol , microbiology and biotechnology , atp hydrolysis , gene , cell , enzyme , chloroplast , thylakoid
Mitochondrial translation of the Saccharomyces cerevisiae Atp6p subunit of F 1 –F 0 ATP synthase is regulated by the F 1 ATPase. Here we show normal expression of Atp6p in HeLa cells depleted of the F 1 β subunit. Instead of being translationally down‐regulated, HeLa cells lacking F 1 degrade Atp6p, thereby preventing proton leakage across the inner membrane. Mammalian mitochondria also differ in the way they minimize the harmful effect of unassembled F 1 α subunit. While yeast mutants lacking β subunit have stable aggregated F 1 α subunit in the mitochondrial matrix, the human α subunit is completely degraded in cells deficient in F 1 β subunit. These results are discussed in light of the different properties of the proteins and environments in which yeast and human mitochondria exist.