Mitochondrial protein import: mechanisms, components and energetics.
The transport of nuclear-encoded proteins from the cytosol into mitochondria is mediated by targeting (signal) sequences present on precursor forms. Most precursors of the mitochondrial matrix possess amino-terminal signals which characteristically contain hydroxylated and basic amino acids and lack acidic residues. With a minority of precursor proteins, internal sequence motifs can direct proteins to the mitochondria (Pfanner, N., Hoeben, P., Tropschug, M. and Neupert, W. (1987) J. Biol. Chem. 262, 14851-14854). The presence of a mitochondrial targeting sequence alone, however, is not sufficient for specific targeting to the organelle and further to the various subcompartments. There is the need for components which recognise the targeting sequences and others which keep the precursor protein in a translocation-competent form. Beyond the recognition step, components are required which mediate translocation across the mitochondrial membranes. Mitochondria posses two translocation machineries, one in the outer membrane and one in the inner membrane. The matrix space harbors a number of factors which participate in the import of proteins, in their unfolding and folding. Energy is required at several steps of these processes.
Schwarz
E
E
Institut für Physiologische Chemie, Universität München, Germany.
Neupert
W
W
D003600:Cytosol / Q000378:metabolism; D004734:Energy Metabolism; D005656:Fungal Proteins / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000378:metabolism; D007425:Intracellular Membranes / Q000378:metabolism*; D008928:Mitochondria / Q000378:metabolism*; D009492:Neurospora crassa; D017510:Protein Folding; D021382:Protein Sorting Signals / Q000378:metabolism
D005656:Fungal Proteins; D006360:Heat-Shock Proteins; D021382:Protein Sorting Signals