A H2O2-producing glyoxal oxidase is required for filamentous growth and pathogenicity in Ustilago maydis.
Identifieur interne : 000862 ( Main/Exploration ); précédent : 000861; suivant : 000863A H2O2-producing glyoxal oxidase is required for filamentous growth and pathogenicity in Ustilago maydis.
Auteurs : B. Leuthner [Allemagne] ; C. Aichinger ; E. Oehmen ; E. Koopmann ; O. Müller ; P. Müller ; R. Kahmann ; M. Bölker ; P H SchreierSource :
- Molecular genetics and genomics : MGG [ 1617-4615 ] ; 2005.
Descripteurs français
- KwdFr :
- Alcohol oxidoreductases (génétique), Alcohol oxidoreductases (physiologie), Haploïdie (MeSH), Maladies des plantes (microbiologie), Mutation (génétique), Méthylglyoxal (métabolisme), Peroxyde d'hydrogène (métabolisme), Phylogenèse (MeSH), Phénotype (MeSH), Protéines membranaires (génétique), Protéines membranaires (physiologie), Protéines végétales (génétique), Protéines végétales (physiologie), Spécificité du substrat (physiologie), Structure tertiaire des protéines (MeSH), Transduction du signal (MeSH), Ustilago (croissance et développement), Ustilago (enzymologie), Ustilago (pathogénicité).
- MESH :
- croissance et développement : Ustilago.
- enzymologie : Ustilago.
- génétique : Alcohol oxidoreductases, Mutation, Protéines membranaires, Protéines végétales.
- microbiologie : Maladies des plantes.
- métabolisme : Méthylglyoxal, Peroxyde d'hydrogène.
- pathogénicité : Ustilago.
- physiologie : Alcohol oxidoreductases, Protéines membranaires, Protéines végétales, Spécificité du substrat.
- Haploïdie, Phylogenèse, Phénotype, Structure tertiaire des protéines, Transduction du signal.
English descriptors
- KwdEn :
- Alcohol Oxidoreductases (genetics), Alcohol Oxidoreductases (physiology), Haploidy (MeSH), Hydrogen Peroxide (metabolism), Membrane Proteins (genetics), Membrane Proteins (physiology), Mutation (genetics), Phenotype (MeSH), Phylogeny (MeSH), Plant Diseases (microbiology), Plant Proteins (genetics), Plant Proteins (physiology), Protein Structure, Tertiary (MeSH), Pyruvaldehyde (metabolism), Signal Transduction (MeSH), Substrate Specificity (physiology), Ustilago (enzymology), Ustilago (growth & development), Ustilago (pathogenicity).
- MESH :
- chemical , genetics : Alcohol Oxidoreductases, Membrane Proteins, Plant Proteins.
- chemical , metabolism : Hydrogen Peroxide, Pyruvaldehyde.
- chemical , physiology : Alcohol Oxidoreductases, Membrane Proteins, Plant Proteins.
- enzymology : Ustilago.
- genetics : Mutation.
- growth & development : Ustilago.
- microbiology : Plant Diseases.
- pathogenicity : Ustilago.
- physiology : Substrate Specificity.
- Haploidy, Phenotype, Phylogeny, Protein Structure, Tertiary, Signal Transduction.
Abstract
In the phytopathogenic fungus Ustilago maydis the mating-type loci control the transition from yeast-like to filamentous growth required for pathogenic development. In a large REMI (restriction enzyme mediated integration) screen, non-pathogenic mutants were isolated in a haploid strain that had been engineered to be pathogenic. In one of these mutants, which showed a specific morphological phenotype, the tagged gene, glo1 , was found to encode a product that is highly homologous to a glyoxal oxidase gene from the wood-rot fungus Phanerochaete chrysosporium. Glyoxal oxidase homologues are found in human, plant pathogenic fungi and in plants, but not in other mammals or yeasts. To confirm the function of the glo1 gene, null mutations were generated in compatible haploid U. maydis strains. In crosses null mutants were unable to generate filamentous dikaryons, and were completely non-pathogenic. Using a Glo1-overproducing strain we demonstrated that Glo1 is membrane bound, oxidizes a series of small aldehydes (< C4) and produces H2O2. The enzyme needs to be activated, presumably by auto-oxidation, to show full activity. A potential role for Glo1 during filamentous growth and pathogenic development of U. maydis is proposed.
DOI: 10.1007/s00438-004-1085-6
PubMed: 15578222
Affiliations:
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In a large REMI (restriction enzyme mediated integration) screen, non-pathogenic mutants were isolated in a haploid strain that had been engineered to be pathogenic. In one of these mutants, which showed a specific morphological phenotype, the tagged gene, glo1 , was found to encode a product that is highly homologous to a glyoxal oxidase gene from the wood-rot fungus Phanerochaete chrysosporium. Glyoxal oxidase homologues are found in human, plant pathogenic fungi and in plants, but not in other mammals or yeasts. To confirm the function of the glo1 gene, null mutations were generated in compatible haploid U. maydis strains. In crosses null mutants were unable to generate filamentous dikaryons, and were completely non-pathogenic. Using a Glo1-overproducing strain we demonstrated that Glo1 is membrane bound, oxidizes a series of small aldehydes (< C4) and produces H2O2. The enzyme needs to be activated, presumably by auto-oxidation, to show full activity. A potential role for Glo1 during filamentous growth and pathogenic development of U. maydis is proposed.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15578222</PMID><DateCompleted><Year>2005</Year><Month>04</Month><Day>15</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">1617-4615</ISSN><JournalIssue CitedMedium="Print"><Volume>272</Volume><Issue>6</Issue><PubDate><Year>2005</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Molecular genetics and genomics : MGG</Title><ISOAbbreviation>Mol Genet Genomics</ISOAbbreviation></Journal><ArticleTitle>A H2O2-producing glyoxal oxidase is required for filamentous growth and pathogenicity in Ustilago maydis.</ArticleTitle><Pagination><MedlinePgn>639-50</MedlinePgn></Pagination><Abstract><AbstractText>In the phytopathogenic fungus Ustilago maydis the mating-type loci control the transition from yeast-like to filamentous growth required for pathogenic development. In a large REMI (restriction enzyme mediated integration) screen, non-pathogenic mutants were isolated in a haploid strain that had been engineered to be pathogenic. In one of these mutants, which showed a specific morphological phenotype, the tagged gene, glo1 , was found to encode a product that is highly homologous to a glyoxal oxidase gene from the wood-rot fungus Phanerochaete chrysosporium. Glyoxal oxidase homologues are found in human, plant pathogenic fungi and in plants, but not in other mammals or yeasts. To confirm the function of the glo1 gene, null mutations were generated in compatible haploid U. maydis strains. In crosses null mutants were unable to generate filamentous dikaryons, and were completely non-pathogenic. Using a Glo1-overproducing strain we demonstrated that Glo1 is membrane bound, oxidizes a series of small aldehydes (< C4) and produces H2O2. The enzyme needs to be activated, presumably by auto-oxidation, to show full activity. A potential role for Glo1 during filamentous growth and pathogenic development of U. maydis is proposed.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Leuthner</LastName><ForeName>B</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Bayer CropScience AG, Alfred-Nobel-Strasse 50, 40789 Monheim, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Aichinger</LastName><ForeName>C</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Oehmen</LastName><ForeName>E</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Koopmann</LastName><ForeName>E</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Müller</LastName><ForeName>O</ForeName><Initials>O</Initials></Author><Author ValidYN="Y"><LastName>Müller</LastName><ForeName>P</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Kahmann</LastName><ForeName>R</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Bölker</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Schreier</LastName><ForeName>P H</ForeName><Initials>PH</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2004</Year><Month>12</Month><Day>01</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Mol Genet Genomics</MedlineTA><NlmUniqueID>101093320</NlmUniqueID><ISSNLinking>1617-4623</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008565">Membrane Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>722KLD7415</RegistryNumber><NameOfSubstance UI="D011765">Pyruvaldehyde</NameOfSubstance></Chemical><Chemical><RegistryNumber>BBX060AN9V</RegistryNumber><NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D000429">Alcohol Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.3.-</RegistryNumber><NameOfSubstance UI="C052371">glyoxal oxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000429" MajorTopicYN="N">Alcohol Oxidoreductases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006238" MajorTopicYN="N">Haploidy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008565" MajorTopicYN="N">Membrane Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010641" MajorTopicYN="N">Phenotype</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010935" MajorTopicYN="N">Plant Diseases</DescriptorName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011765" MajorTopicYN="N">Pyruvaldehyde</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014588" MajorTopicYN="N">Ustilago</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & 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Aichinger</name><name sortKey="Bolker, M" sort="Bolker, M" uniqKey="Bolker M" first="M" last="Bölker">M. Bölker</name><name sortKey="Kahmann, R" sort="Kahmann, R" uniqKey="Kahmann R" first="R" last="Kahmann">R. Kahmann</name><name sortKey="Koopmann, E" sort="Koopmann, E" uniqKey="Koopmann E" first="E" last="Koopmann">E. Koopmann</name><name sortKey="Muller, O" sort="Muller, O" uniqKey="Muller O" first="O" last="Müller">O. Müller</name><name sortKey="Muller, P" sort="Muller, P" uniqKey="Muller P" first="P" last="Müller">P. Müller</name><name sortKey="Oehmen, E" sort="Oehmen, E" uniqKey="Oehmen E" first="E" last="Oehmen">E. Oehmen</name><name sortKey="Schreier, P H" sort="Schreier, P H" uniqKey="Schreier P" first="P H" last="Schreier">P H Schreier</name></noCountry><country name="Allemagne"><noRegion><name sortKey="Leuthner, B" sort="Leuthner, B" uniqKey="Leuthner B" first="B" last="Leuthner">B. 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