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MBE Advance Access published online on April 27, 2005
Molecular Biology and Evolution, doi:10.1093/molbev/msi151
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© The Author 2005. 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@oupjournals.org
Accepted April 18, 2005

Letter

Reciprocal Fusions of Two Genes in the Formaldehyde Detoxification Pathway in Ciliates and Diatoms

Nicholas A. Stover 1*, André R. O. Cavalcanti 2, Anya J. Li 2, Brian C. Richardson 2, and Laura F. Landweber 2

1 Department of Ecology and Evolutionary Biology, Princeton University, Princeton, NJ 08544; Current address: Department of Genetics, Stanford University School of Medicine, Stanford, CA 94305-5120
2 Department of Ecology and Evolutionary Biology, Princeton University, Princeton, NJ 08544

* To whom correspondence should be addressed.
Nicholas A. Stover, E-mail: nick{at}genome.stanford.edu


  Abstract

During the course of a pilot genome project for the ciliate Oxytricha trifallax, we discovered a fusion gene never before described in any taxa. This gene, FSF1, encodes a putative fusion protein comprised of an entire formaldehyde dehydrogenase (FALDH) homolog at one end and an S-formylglutathione hydrolase (SFGH) homolog at the other, two proteins that catalyze serial steps in the formaldehyde detoxification pathway. We confirmed the presence of the Oxytricha fusion gene in vivo and detected transcripts of the full-length fusion gene. A survey of other large-scale sequencing projects revealed a similar fusion protein in a distantly related ciliate, Tetrahymena thermophila, and a possible fusion of these two genes in the diatoms Phaeodactylum tricornutum and Thalassiosira pseudonana, but in the reverse order, with the SFGH domain encoded upstream of the FALDH domain. Orthologs of these fusion proteins may be widespread within the ciliates and diatoms, respectively.

Keywords: Fusion Gene; Formaldehyde Dehydrogenase; S-Formylglutathione Hydrolase; Alcohol Dehydrogenase III; Esterase D; Bikont Phylogeny.
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