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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Aspergillus fumigatus / enzymology*
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Aspergillus fumigatus / genetics
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Cloning, Molecular*
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Dinitrochlorobenzene / pharmacology
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Escherichia coli / enzymology
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Escherichia coli / genetics
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Fungal Proteins / genetics
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Fungal Proteins / metabolism
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Gene Expression Regulation, Fungal*
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Glutathione Transferase* / chemistry
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Glutathione Transferase* / genetics
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Glutathione Transferase* / metabolism
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Humans
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Hydrogen Peroxide / pharmacology
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Molecular Sequence Data
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Oxidative Stress
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Phylogeny
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Sequence Alignment
Substances
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Dinitrochlorobenzene
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Fungal Proteins
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Recombinant Proteins
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Hydrogen Peroxide
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Glutathione Transferase
Associated data
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GENBANK/AY770043
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GENBANK/AY770044
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GENBANK/AY770045
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GENBANK/AY770046