Cloning and expression of an iron-containing superoxide dismutase in the parasitic protist, Trichomonas vaginalis.
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.
Viscogliosi
E
E
Laboratoire de Biologie des Protistes, UPRESA 6023 CNRS, Aubière, France. viscogliosi@cicsun.univ-bpclermont.fr
Delgado-Viscogliosi
P
P
Gerbod
D
D
Dauchez
M
M
Gratepanche
S
S
Alix
A J
AJ
Dive
D
D
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D018628:Gene Dosage; D007501:Iron; D008969:Molecular Sequence Data; D010802:Phylogeny; D017433:Protein Structure, Secondary; D013482:Superoxide Dismutase / Q000737:chemistry / Q000235:genetics*; D014246:Trichomonas vaginalis / Q000201:enzymology* / Q000235:genetics
D007501:Iron; D013482:Superoxide Dismutase