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MBE Advance Access published online on May 21, 2004
Molecular Biology and Evolution, doi:10.1093/molbev/msh166
Molecular Biology and Evolution © Society for Molecular Biology and Evolution 2004; all rights reserved
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Accepted May 11, 2004

Original Articles

Tom22', an 8 kDa trans-Site Receptor in Plants and Protozoans, Is a Conserved Feature of the TOM Complex that Appeared Early in the Evolution of Eukaryotes

Diana Macasev 1, James Whelan 2, Ed Newbigin 3, Marcio C. Silva-Filho 4, Terrence D. Mulhern 1, Trevor Lithgow 1

1 Russell Grimwade School of Biochemistry and Molecular Biology, University of Melbourne, Parkville 3010, Australia
2 Plant Molecular Biology Group, School of Biomedical and Chemical Sciences, University of Western Australia, Crawley 6009, Australia
3 School of Botany, University of Melbourne, Parkville 3010, Australia
4 Russell Grimwade School of Biochemistry and Molecular Biology, University of Melbourne, Parkville 3010, Australia; Departamento de Genetica, Escola Superior de Agricultura Luiz de Queiroz, Universidade de Sao Paulo, C.P. 83, 13400-970 Piracicaba, SP, Brazil


  Abstract

One of the earliest events in the evolution of mitochondria was to devise a means to translocate proteins made in the cytosol into the "proto-mitochondrion". How this was achieved remains uncertain and the nature of the earliest version of the protein translocation machinery is not known. Comparative sequence analysis suggests three subunits, Tom40, Tom7 and Tom22 as common elements of the protein translocase in the mitochondrial outer membrane in diverse extant eukaryotes. Tom22, the 22 kDa subunit, plays a critical role in the function of this complex in fungi and animals, and we show that an 8 kDa subunit of the plant translocase is a truncated form of Tom22: it has a single transmembrane segment conforming in sequence to the same region of Tom22 from other eukaryotic lineages and a short carboxy-terminal trans domain located in the mitochondrial intermembrane space. The trans domain from the Arabidopsis thaliana protein functions in yeast lacking their own Tom22, complementing protein import defects and restoring cell growth. Moreover, we have identified orthologs of Tom22, Tom7 and Tom40 in diverse eukaryotes such as the diatom Phaeodactylum tricornutum, the amoebic slime Dictyostelium discoideum and the protozoan parasite Plasmodium falciparum. This strongly suggests these subunits as the core of the protein translocase in the earliest mitochondria.

Key Words: mitochondria, protein import, TOM complex, evolution


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