Abstract
Protein translocation across membranes is a fundamental cellular process that is especially vital for mitochondrial biogenesis. More than 95% of all mitochondrial proteins must be imported from the cytoplasm. The protein-translocating channels of mitochondria have many identical properties including conductance, voltage dependence and regulation by synthetic peptides whose sequences mimic the targeting domains of precursors. Viewing protein translocation across membranes as movement of polymers through confined pathways has provided a novel perspective of channel function. These considerations suggest the observed flickering of the channels in the presence of targeting peptides represents an interaction of the peptides with the channel rather than translocation events.
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Kinnally, K.W. (2002). Protein Translocation Channels in Mitochondria. In: Kasianowicz, J.J., Kellermayer, M.S.Z., Deamer, D.W. (eds) Structure and Dynamics of Confined Polymers. NATO Science Series, vol 87. Springer, Dordrecht. https://doi.org/10.1007/978-94-010-0401-5_5
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DOI: https://doi.org/10.1007/978-94-010-0401-5_5
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