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Formaldehyde dehydrogenase/S-formylglutathione hydrolase fusion protein; fusion protein containing two enzymes known to catalyze sequential steps in the formaldehyde detoxification pathway in yeast; this fusion unique to ciliates
SFA1 Bifunctional enzyme conta
ining both alcohol dehydrogena
se and glutathione-dependent f
ormaldehyde dehydrogenase acti
vities, functions in formaldeh
yde detoxification and formati
on of long chain and complex a
lcohols, regulated by Hog1p-Sk
o1p
A macronuclear chromosome containing a fusion gene was cloned from the spirotrichous ciliate Oxytricha trifallax. The gene encodes a single polypeptide containing homologs of two proteins that catalyze sequential steps in the formaldehyde detoxification pathway in Saccharomyces cerevisiae. These two proteins are formaldehyde dehydrogenase (FALDH) and S-formylglutathione hydrolase (SFGH); the fusion gene is called FSF1 (FALDH/SFGH Fusion 1). A similar gene was identified in the Tetrahymena thermophila genome sequence, and a T. thermophila EST sequenced from both ends showed that the fusion gene is expressed in this species in vivo. FSF1 has not yet been identified in other ciliates, but a fusion of these two genes has been identified in another group of protists, the diatoms. An EST from Phaeodactylum tricornutum and a gene from the genome sequence of Thalassiosira pseudonana both encode a fusion of these two genes, but in the opposite orientation of the ciliate genes. In diatoms, the SFGH domain is found N-terminal to the FALDH domain, suggesting that these two fusion genes evolved independently in ciliates and diatoms. The diatom genes were named SFF1 to highlight these differences.
Associated Literature
Ref:15858209: Stover NA, Cavalcanti AR, Li AJ, Richardson BC, Landweber LF (2005) Reciprocal fusions of two genes in the formaldehyde detoxification pathway in ciliates and diatoms. Molecular biology and evolution 22(7):1539-42
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