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Mitochondrial protein import

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Abstract

Most polypeptides of mitochondria are imported from the cytosol. Precursor proteins contain targeting and sorting information, often in the form of amino-terminal presequences. Precursors first bind to receptors in the outer membrane. Two putative import receptors have been identified: a 19-kilodalton protein (MOM19) inNeurospora mitochondria, and a 70-kilodalton protein (MAS70) in yeast. Some precursors integrate directly into the outer membrane, but the majority are translocated through one or both membranes. This process requires an electrochemical potential across the inner membrane. Import appears to occur through a hydrophilic pore, although the inner and outer membranes may contain functionally separate translocation machineries. In yeast, a 42-kilodalton protein (ISP42) probably forms part of the outer membrane channel. After import, precursors interact with “chaperonin” ATPases in the matrix. Presequences then are removed by the matrix protease. Finally, some proteins are retranslocated across the inner membrane to the intermembrane space.

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Authors and Affiliations

  1. Centre de Biochimie et de Biologie Moléculaire, C.N.R.S., Marseilles, France

    Vincent Geli

  2. Biocenter, University of Basel, CH-4056, Basel, Switzerland

    Benjamin Glick

Authors
  1. Vincent Geli
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  2. Benjamin Glick
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Geli, V., Glick, B. Mitochondrial protein import. J Bioenerg Biomembr 22, 725–751 (1990). https://doi.org/10.1007/BF00786928

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  • DOI: https://doi.org/10.1007/BF00786928

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