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The presence of four iron-containing superoxide dismutase isozymes in Trypanosomatidae: Characterization, subcellular localization, and phylogenetic origin in Trypanosoma brucei

Lookup NU author(s): Dr Christophe Noel


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Metalloenzymes such as the superoxide dismutases (SODs) form part of a defense mechanism that helps protect obligate and facultative aerobic organisms from oxygen toxicity and damage. Here, we report the presence in the trypanosomatid genomes of four SOD genes: soda, sodb1, sodb2, and a newly identified sodc. All four genes of Trypanosoma brucei have been cloned (Tbsods), sequenced, and overexpressed in Escherichia coli and shown to encode active dimeric FeSOD isozymes. Homology modeling of the structures of all four enzymes using available X-ray crystal structures of homologs showed that the four TbSOD structures were nearly identical. Subcellular localization using GFP-fusion proteins in procyclic insect trypomastigotes shows that TbSODB1 is mainly cytosolic, with a minor glycosomal component, TbSODB2 is mainly glycosomal with some activity in the cytosol, and TbSODA and TbSODC are both mitochondrial isozymes. Phylogenetic studies of all available trypanosomatid SODs and 106 dimeric FeSODs and closely related cambialistic dimeric SOD sequences suggest that the trypanosomatid SODs have all been acquired by more than one event of horizontal gene transfer, followed by events of gene duplication. © 2005 Elsevier Inc. All rights reserved.

Publication metadata

Author(s): Dufernez F, Yernaux C, Gerbod D, Noel C, Chauvenet M, Wintjens R, Edgcomb VP, Capron M, Opperdoes FR, Viscogliosi E

Publication type: Article

Publication status: Published

Journal: Free Radical Biology and Medicine

Year: 2006

Volume: 40

Issue: 2

Pages: 210-225

ISSN (print): 0891-5849

ISSN (electronic): 1873-4596

Publisher: Elsevier


DOI: 10.1016/j.freeradbiomed.2005.06.021

PubMed id: 16413404


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