Browse by author
Lookup NU author(s): Dr Christophe Noel
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
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.
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
URL: http://dx.doi.org/10.1016/j.freeradbiomed.2005.06.021
DOI: 10.1016/j.freeradbiomed.2005.06.021
PubMed id: 16413404
Altmetrics provided by Altmetric