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MBE Advance Access published online on June 22, 2007
Molecular Biology and Evolution, doi:10.1093/molbev/msm126
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© The Author 2007. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Letter

Domain Stealing by Receptors in a Protein Transport Complex

Joanne M. Hulett1, Peter Walsh1 and Trevor Lithgow*

Department of Biochemistry and Molecular Biology, and Bio21 Molecular Sciences and Biotechnology Institute, University of Melbourne, Parkville 3010, Australia

* To whom correspondence should be addressed: phone: 61 3 8344 2312 , fax: 61 3 9348 1421, t.lithgow{at}unimelb.edu.au

Received for publication April 12, 2007. Revision received June 3, 2007. Accepted for publication June 18, 2007.

The mitochondrion is an essential cellular compartment in eukaryotes. The mitochondrial proteins Tom20 and Tom22 are receptors that ensure recognition and binding of proteins imported for mitochondrial biogenesis. Comparison of the sequence for the Tom20 and Tom22 subunits in the yeasts Saccharomyces cerevisiae and Saccharomyces castellii, show a rare case of domain stealing, where in Saccharomyces castellii Tom22 has lost an acidic domain, and Tom20 has gained one. This example of domain stealing is a snapshot of evolution in action and provides excellent evidence that Tom20 and Tom22 are subunits of a single, composite receptor that binds precursor proteins for import into mitochondria.

1 These authors contributed equally.


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