| Literature DB >> 15749051 |
Claire Burns1, Rachel Geraghty, Claire Neville, Alan Murphy, Kevin Kavanagh, Sean Doyle.
Abstract
Analysis of the genome of the human pathogen, Aspergillus fumigatus, revealed the presence of several putative glutathione transferase (GST) open reading frames. Three A. fumigatus GST genes, termed gstA, B, and C, were cloned and recombinant proteins expressed in Escherichia coli. Functional analysis of recombinant gstA-C confirms that the enzymes exhibit GST activity and glutathione peroxidase activity. RT-PCR confirmed low basal expression of gstA and gstC which was markedly up-regulated (at least 4x-10x) in the presence of either H2O2 or 1-chloro-2,4-dinitrobenzene (CDNB). GstB expression was only observed in the presence of CDNB. These results demonstrate for the first time the existence of three functional GSTs in A. fumigatus and strongly suggest a role for these enzymes in the response of the organism to both oxidative stress and xenobiotic presence.Entities:
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Year: 2005 PMID: 15749051 DOI: 10.1016/j.fgb.2005.01.001
Source DB: PubMed Journal: Fungal Genet Biol ISSN: 1087-1845 Impact factor: 3.495