Mitochondrial targeting signals matrix proteins

This a-helix is amphipathic, containing patches of positively charged and hydrophobic amino acids, respectively, on opposite surfaces of the theoretical cylinder. The presequence is usually processed by the mitochondrial processing peptidase (MPP) and the mature protein is sorted to either the matrix, or to the inner membrane if it bears a hydrophobic stop-transfer sequence. Some mitochondrial proteins, mostly destined to the membranes, do not have cleavable N-terminal presequences but have internal targeting signals that are not well characterized (Pfanner and Geissler 2001). 

Most mitochondria and chloroplast proteins are made on free cytosolic ribosomes, released into the cytosol and then taken up into the organelle. Uptake into the mitochondrial matrix requires a matrix-targeting sequence and occurs at sites where the outer and inner mitochondrial membranes come into contact. The process is mediated by hsp70 and hsp60 proteins and requires both ATP hydrolysis and an electrochemical gradient across the inner mitochondrial membrane. Targeting of proteins to other compartments of mitochondria or chloroplasts requires two signals. 

Roise, D and Maduke, M. (1994) Import of a Mitochondrial Presequence into P. Denitrificans, FEBS Letters, 337, 9-13 Cavalier-Smith, T. (1987) The Simultaneous Symbiotic Origin of Mitochondria, Chloroplasts and Microbodies, Annals of the New York Academy of Science, 503, 55-71 Cavalier-Smith, T. (1992) The Number of Symbiotic Origins of Organelles, BioSystems, 28, 91-106 Hartl, F Ostermann, J., Guiard, B and Neupert, W. (1987) Successive Translocation into and out of the Mitochondrial Matrix Targeting of Proteins to the Inner Membrane Space by a Bipartite Signal Peptide, Cell, 51,1027-1037. 

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