What fuels polypeptide translocation? An energetical view on mitochondrial protein sorting.
Protein sorting into mitochondria is achieved by the concerted action of at least four translocation complexes. Vectorial transport of polypeptide chains by these complexes requires different driving forces. In particular, Deltapsi, matrix adenosine triphosphate and the free energy of the binding to other protein components are used in series to achieve sorting of proteins to the various mitochondrial subcompartments. The processes providing the translocation energy are presented in this review and their impact for protein sorting into and within mitochondria is discussed.
Herrmann
J M
JM
Institut für Physiologische Chemie, Goethestrasse 33, 80336, München, Germany.
Neupert
W
W
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000378:metabolism*; D029968:Escherichia coli Proteins; D005057:Eukaryotic Cells; D007425:Intracellular Membranes / Q000378:metabolism*; D008564:Membrane Potentials; D026901:Membrane Transport Proteins; D008928:Mitochondria / Q000737:chemistry / Q000378:metabolism*; D020409:Molecular Motor Proteins; D011485:Protein Binding; D017510:Protein Folding; D021381:Protein Transport; D000069816:SEC Translocation Channels; D000081416:SecA Proteins
D001426:Bacterial Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; D020409:Molecular Motor Proteins; D000069816:SEC Translocation Channels; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D000081416:SecA Proteins