
Cloning and expression of an iron‐containing superoxide dismutase in the parasitic protist, Trichomonas vaginalis
Author(s) -
Viscogliosi Eric,
DelgadoViscogliosi Pilar,
Gerbod Delphine,
Dauchez Manuel,
Gratepanche Sylvie,
Alix Alain J.P,
Dive Daniel
Publication year - 1998
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1998.tb12936.x
Subject(s) - trichomonas vaginalis , biology , gene , protist , escherichia coli , superoxide dismutase , microbiology and biotechnology , cloning (programming) , giardia , biochemistry , enzyme , programming language , computer science
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.