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. 1987 Aug;6(8):2433–2439. doi: 10.1002/j.1460-2075.1987.tb02522.x

Transport of proteins to the mitochondrial intermembrane space: the 'matrix-targeting' and the 'sorting' domains in the cytochrome c1 presequence.

A P van Loon 1, A W Brändli 1, B Pesold-Hurt 1, D Blank 1, G Schatz 1
PMCID: PMC553650  PMID: 2822392

Abstract

We reported earlier that the yeast cytochrome c1 presequence (length: 61 amino acids) directs attached proteins to the mitochondrial intermembrane space and that it appears to contain two functional domains: a 'matrix-targeting' domain, and a 'sorting' domain. We have now used gene manipulation together with two different in vivo import assays to map these two domains within the cytochrome c1 presequence. The 'matrix-targeting' domain is contained within the N-terminal 16 residues (or less); by itself, it directs attached proteins to the matrix. The 'sorting' domain extends into the C-terminal 13 residues of the presequence; while it does not mediate intracellular protein transport by itself, it acts together with the preceding 'matrix-targeting' sequence in sorting attached proteins into the intermembrane space. On replacing the authentic 'matrix-targeting' sequence with artificial sequences of different lengths we found that sorting of proteins between the outer membrane and the intermembrane space is not exclusively determined by the length of the N-terminal 'matrix-targeting' sequence.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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