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Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria
Author(s) -
Chen Ruming,
Runswick Michael J.,
Carroll Joe,
Fearnley Ian M.,
Walker John E.
Publication year - 2007
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.2007.05.079
Subject(s) - atp synthase , atpase , mitochondrion , biochemistry , biology , protein subunit , enzyme , atp synthase gamma subunit , atp–adp translocase , function (biology) , microbiology and biotechnology , chemistry , inner mitochondrial membrane , atp hydrolysis , gene
ATP synthase, or F‐ATPase, purified from bovine heart mitochondria in the absence of phospholipids is an assembly of 16 different subunits. In the presence of exogenous phospholipids, two additional hydrophobic proteins, a 6.8 kDa proteolipid and diabetes associated protein in insulin sensitive tissue (DAPIT), were associated with the purified complex, with DAPIT at sub‐stoichiometric levels. Both proteins are conserved in vertebrates and invertebrates, but not in fungi, and prokaryotic F‐ATPases do not contain orthologues of either of them. Therefore, their roles are likely to be peripheral to the synthesis of ATP.