Viscogliosi E, Delgado-Viscogliosi P, Gerbod D, Dauchez M, Gratepanche S, Alix A J, Dive D
Laboratoire de Biologie des Protistes, UPRESA 6023 CNRS, Aubière, France.
FEMS Microbiol Lett. 1998 Apr 1;161(1):115-23. doi: 10.1111/j.1574-6968.1998.tb12936.x.
A superoxide dismutase (SOD) gene of the parasitic protist Trichomonas vaginalis was cloned, sequenced, expressed in Escherichia coli, and its gene product characterized. It is an iron-containing dimeric protein with a monomeric mass of 22,067 Da. Southern blots analyses suggested the presence of seven iron-containing (FeSOD) gene copies. Hydrophobic cluster analysis revealed some peculiarities in the 2D structure of the FeSOD from T. vaginalis and a strong structural conservation between prokaryotic and eukaryotic FeSODs. Phylogenetic reconstruction of the SOD sequences confirmed the dichotomy between FeSODs and manganese-containing SODs. FeSODs of protists appeared to group together with homologous proteobacterial enzymes suggesting a possible origin of eukaryotic FeSODs through an endosymbiotic event.