Schneider H, Söllner T, Dietmeier K, Eckerskorn C, Lottspeich F, Trülzsch B, Neupert W, Pfanner N
Institut für Physiologische Chemie, Universität München, Germany.
Science. 1991 Dec 13;254(5038):1659-62. doi: 10.1126/science.1661031.
The targeting of proteins to mitochondria involves the recognition of the precursor proteins by receptors on the mitochondrial surface followed by insertion of the precursors into the outer membrane at the general insertion site GIP. Most mitochondrial proteins analyzed so far use a mitochondrial outer membrane protein of 19 kilodaltons (MOM19) as an import receptor. The gene encoding MOM19 has now been isolated. The deduced amino acid sequence predicts that MOM19 is anchored in the outer membrane by an NH2-terminal hydrophobic sequence, while the rest of the protein forms a hydrophilic domain exposed to the cytosol. MOM19 was targeted to the mitochondria via a pathway that is independent of protease-accessible surface receptors and controlled by direct assembly of the MOM19 precursor with GIP.
