Cu,Zn superoxide dismutase and zinc stress in the metal-tolerant ericoid mycorrhizal fungus Oidiodendron maius Zn.
Identifieur interne : 002A26 ( Main/Corpus ); précédent : 002A25; suivant : 002A27Cu,Zn superoxide dismutase and zinc stress in the metal-tolerant ericoid mycorrhizal fungus Oidiodendron maius Zn.
Auteurs : Marta Vallino ; Elena Martino ; Francesca Boella ; Claude Murat ; Marco Chiapello ; Silvia PerottoSource :
- FEMS microbiology letters [ 1574-6968 ] ; 2009.
English descriptors
- KwdEn :
- Ascomycota (drug effects), Ascomycota (enzymology), Ascomycota (genetics), Ascomycota (physiology), Copper (pharmacology), Fungal Proteins (genetics), Fungal Proteins (metabolism), Gene Expression Regulation, Fungal (MeSH), Heat-Shock Response (MeSH), Metals, Heavy (pharmacology), Molecular Sequence Data (MeSH), Mutation (MeSH), Mycorrhizae (MeSH), Phylogeny (MeSH), Plant Roots (microbiology), Sequence Analysis, DNA (MeSH), Superoxide Dismutase (genetics), Superoxide Dismutase (metabolism), Transcription, Genetic (MeSH), Vaccinium (microbiology), Zinc (pharmacology).
- MESH :
- chemical , genetics : Fungal Proteins, Superoxide Dismutase.
- chemical , metabolism : Fungal Proteins, Superoxide Dismutase.
- chemical , pharmacology : Copper, Metals, Heavy, Zinc.
- drug effects : Ascomycota.
- enzymology : Ascomycota.
- genetics : Ascomycota.
- microbiology : Plant Roots, Vaccinium.
- physiology : Ascomycota.
- Gene Expression Regulation, Fungal, Heat-Shock Response, Molecular Sequence Data, Mutation, Mycorrhizae, Phylogeny, Sequence Analysis, DNA, Transcription, Genetic.
Abstract
The sequence encoding a superoxide dismutase (SOD) was isolated from the cDNA library of a zinc-tolerant strain of the ericoid mycorrhizal fungus Oidiodendron maius, grown under zinc-stress conditions. Sequence homology to other SODs strongly suggests that it is a copper- and zinc-containing SOD. Functional complementation assays showed that the gene confers increased tolerance to zinc and copper stress to a Cu,ZnSOD-defective yeast mutant. Monitoring of transcript and protein levels following zinc stress suggests that OmSOD1 expression is controlled at the transcriptional level. The OmSod1 protein was found both in the cell extract and in the growth medium of viable fungal cultures. This is the first characterization of an extracellular Cu,ZnSOD in a mycorrhizal fungus. In nature, the presence of OmSod1 in the extracellular environment may also extend the protective role of this enzyme to the plant symbiont. This may be of particular interest from the perspective of using mycorrhizal fungi in bioremediation programmes.
DOI: 10.1111/j.1574-6968.2009.01503.x
PubMed: 19278525
Links to Exploration step
pubmed:19278525Le document en format XML
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Marco" uniqKey="Chiapello M" first="Marco" last="Chiapello">Marco Chiapello</name></author><author><name sortKey="Perotto, Silvia" sort="Perotto, Silvia" uniqKey="Perotto S" first="Silvia" last="Perotto">Silvia Perotto</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:19278525</idno><idno type="pmid">19278525</idno><idno type="doi">10.1111/j.1574-6968.2009.01503.x</idno><idno type="wicri:Area/Main/Corpus">002A26</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002A26</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Cu,Zn superoxide dismutase and zinc stress in the metal-tolerant ericoid mycorrhizal fungus Oidiodendron maius Zn.</title><author><name sortKey="Vallino, Marta" sort="Vallino, Marta" uniqKey="Vallino M" first="Marta" last="Vallino">Marta Vallino</name><affiliation><nlm:affiliation>Dipartimento di Biologia 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type="chemical" qualifier="genetics" xml:lang="en"><term>Fungal Proteins</term><term>Superoxide Dismutase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fungal Proteins</term><term>Superoxide Dismutase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Copper</term><term>Metals, Heavy</term><term>Zinc</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Ascomycota</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Ascomycota</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Ascomycota</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Plant Roots</term><term>Vaccinium</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Ascomycota</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Gene Expression Regulation, Fungal</term><term>Heat-Shock Response</term><term>Molecular Sequence Data</term><term>Mutation</term><term>Mycorrhizae</term><term>Phylogeny</term><term>Sequence Analysis, DNA</term><term>Transcription, Genetic</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The sequence encoding a superoxide dismutase (SOD) was isolated from the cDNA library of a zinc-tolerant strain of the ericoid mycorrhizal fungus Oidiodendron maius, grown under zinc-stress conditions. Sequence homology to other SODs strongly suggests that it is a copper- and zinc-containing SOD. Functional complementation assays showed that the gene confers increased tolerance to zinc and copper stress to a Cu,ZnSOD-defective yeast mutant. Monitoring of transcript and protein levels following zinc stress suggests that OmSOD1 expression is controlled at the transcriptional level. The OmSod1 protein was found both in the cell extract and in the growth medium of viable fungal cultures. This is the first characterization of an extracellular Cu,ZnSOD in a mycorrhizal fungus. In nature, the presence of OmSod1 in the extracellular environment may also extend the protective role of this enzyme to the plant symbiont. This may be of particular interest from the perspective of using mycorrhizal fungi in bioremediation programmes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19278525</PMID><DateCompleted><Year>2009</Year><Month>04</Month><Day>02</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1574-6968</ISSN><JournalIssue CitedMedium="Internet"><Volume>293</Volume><Issue>1</Issue><PubDate><Year>2009</Year><Month>Apr</Month></PubDate></JournalIssue><Title>FEMS microbiology letters</Title><ISOAbbreviation>FEMS Microbiol Lett</ISOAbbreviation></Journal><ArticleTitle>Cu,Zn superoxide dismutase and zinc stress in the metal-tolerant ericoid mycorrhizal fungus Oidiodendron maius Zn.</ArticleTitle><Pagination><MedlinePgn>48-57</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/j.1574-6968.2009.01503.x</ELocationID><Abstract><AbstractText>The sequence encoding a superoxide dismutase (SOD) was isolated from the cDNA library of a zinc-tolerant strain of the ericoid mycorrhizal fungus Oidiodendron maius, grown under zinc-stress conditions. Sequence homology to other SODs strongly suggests that it is a copper- and zinc-containing SOD. Functional complementation assays showed that the gene confers increased tolerance to zinc and copper stress to a Cu,ZnSOD-defective yeast mutant. Monitoring of transcript and protein levels following zinc stress suggests that OmSOD1 expression is controlled at the transcriptional level. The OmSod1 protein was found both in the cell extract and in the growth medium of viable fungal cultures. This is the first characterization of an extracellular Cu,ZnSOD in a mycorrhizal fungus. In nature, the presence of OmSod1 in the extracellular environment may also extend the protective role of this enzyme to the plant symbiont. 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