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A signal-anchor sequence selective for the mitochondrial outer membrane.

H M McBride1, D G Millar, J M Li

  • 1Department of Biochemistry, McGill University, Montreal, Canada.

The Journal of Cell Biology
|December 1, 1992
PubMed
Summary

The outer mitochondrial membrane

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Area of Science:

  • Mitochondrial biogenesis
  • Protein targeting and translocation

Background:

  • Mitochondrial outer membrane proteins require specific targeting signals.
  • The OMM70 protein from yeast possesses a topogenic sequence for outer membrane insertion.

Purpose of the Study:

  • To investigate the role of the NH2-terminal topogenic sequence of OMM70 in targeting and insertion into the mitochondrial outer membrane.
  • To characterize the functional domains within the topogenic sequence responsible for mitochondrial import.

Main Methods:

  • Construction of a hybrid protein (pOMD29) fusing the OMM70 topogenic sequence to dihydrofolate reductase.
  • In vitro import assays using isolated rat heart mitochondria.
  • Analysis of protein import efficiency with varying deletions in the topogenic sequence.

Main Results:

  • The transmembrane segment (amino acids 11-29) alone mediated targeting and insertion into the outer mitochondrial membrane.
  • The NH2-terminal basic region (amino acids 1-10) enhanced the import rate, with basic residues at positions 2, 7, and 9 being crucial.
  • Deletion of amino acids 16-29 abolished in vitro import, highlighting the importance of the transmembrane segment.

Conclusions:

  • The NH2-terminal 29 amino acids of OMM70 function as a signal-anchor sequence for mitochondrial outer membrane sorting.
  • Structural domains within this signal-anchor sequence cooperate for efficient and correct insertion.
  • Mitochondrial outer membrane protein import may involve distinct mechanisms compared to matrix protein import.

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