Ionic mitochondrial channels: characteristics and possible role in protein translocation.

Biochimie
J P HenryM Thieffry

Abstract

Most of the mitochondrial proteins are synthesized in the cytoplasm as precursors which are then translocated into the organelle. These precursors have a NH2-terminal extension which functions as a mitochondrial targeting signal. The import process through mitochondrial membranes is voltage-dependent; its mechanism is still unknown. Translocation has been proposed to occur through specific channels, thus, indicating the interest of the study of mitochondrial ionic channels. Two anion channels with different electrical characteristics have been described in the outer and the inner membranes. Using the technique of "Tip-Dip", we have shown the existence of a cation channel of large conductance in mitochondria. The characteristics of this channel differ from that of the other mitochondrial anion channels. A positively charged 13-residue synthetic peptide, with the sequence of the amino terminal extremity of the nuclear-coded subunit IV of yeast cytochrome C oxidase, induces a blockade of the cationic channel. From the characteristics of the blockade, it is likely that the channel could be permeable to the peptide. The specificity of this effect suggests that this channel might be involved in protein translocation.

References

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Mar 1, 1985·Proceedings of the National Academy of Sciences of the United States of America·D H HochL L Simpson

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Citations

Oct 25, 2006·Annual Review of Physiology·Brian O'Rourke
Feb 28, 1991·Biochemical and Biophysical Research Communications·G CostaJ J Diwan
Apr 3, 2014·Physiological Reviews·Ildiko Szabo, Mario Zoratti
May 23, 1997·The Journal of Biological Chemistry·Y Lu, A D Beavis
May 6, 2016·Journal of Bioenergetics and Biomembranes·María Luisa CampoSonia Martínez-Caballero
Jan 12, 2001·Physiological Reviews·M MazzantiH Oberleithner

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