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Molecular chaperones

Plugging the transport gap

Nature volume 421, pages 801–802 (2003)Cite this article

Molecular chaperones are generally thought to protect newly synthesized proteins and ensure that they fold into the correct shape. But it seems that two chaperones also help to target certain proteins to mitochondria.

Mitochondrial preproteins face several problems. After they have been released from ribosomes, they must be targeted to mitochondria but not to other organelles in the cell. They must also adopt conformations that can unfold easily, because they move as extended chains through the two membranes (outer and inner) that surround mitochondria. Such incompletely folded proteins often display hydrophobic regions on their surface, especially if they are membrane proteins, creating the danger of self-aggregation. These problems are combated by molecular chaperones, a large class of proteins that assist the correct folding and assembly of other proteins without remaining bound to them once they are performing their normal functions4.

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Figure 1: Targeting proteins to mitochondria, as proposed by Young et al.1.

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  1. Department of Biological Sciences, University of Warwick, Coventry, CV4 7AL, UK

    R. John Ellis

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  1. R. John Ellis
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Correspondence to R. John Ellis.

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Ellis, R. Plugging the transport gap. Nature 421, 801–802 (2003). https://doi.org/10.1038/421801a

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