Identification of PAD2 as a gamma-glutamylcysteine synthetase highlights the importance of glutathione in disease resistance of Arabidopsis.
Identifieur interne : 001E49 ( Main/Exploration ); précédent : 001E48; suivant : 001E50Identification of PAD2 as a gamma-glutamylcysteine synthetase highlights the importance of glutathione in disease resistance of Arabidopsis.
Auteurs : Vincent Parisy [Suisse] ; Benoit Poinssot ; Lucas Owsianowski ; Antony Buchala ; Jane Glazebrook ; Felix MauchSource :
- The Plant journal : for cell and molecular biology [ 0960-7412 ] ; 2007.
Descripteurs français
- KwdFr :
- Arabidopsis (génétique), Arabidopsis (microbiologie), Arabidopsis (métabolisme), Données de séquences moléculaires (MeSH), Glutamate-cysteine ligase (génétique), Glutamate-cysteine ligase (métabolisme), Glutathion (métabolisme), Maladies des plantes (microbiologie), Phytophthora (physiologie), Pseudomonas syringae (physiologie), Séquence d'acides aminés (MeSH).
- MESH :
- génétique : Arabidopsis, Glutamate-cysteine ligase.
- microbiologie : Arabidopsis, Maladies des plantes.
- métabolisme : Arabidopsis, Glutamate-cysteine ligase, Glutathion.
- physiologie : Phytophthora, Pseudomonas syringae.
- Données de séquences moléculaires, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Arabidopsis (genetics), Arabidopsis (metabolism), Arabidopsis (microbiology), Glutamate-Cysteine Ligase (genetics), Glutamate-Cysteine Ligase (metabolism), Glutathione (metabolism), Molecular Sequence Data (MeSH), Phytophthora (physiology), Plant Diseases (microbiology), Pseudomonas syringae (physiology).
- MESH :
- chemical , genetics : Glutamate-Cysteine Ligase.
- genetics : Arabidopsis.
- metabolism : Arabidopsis, Glutamate-Cysteine Ligase, Glutathione.
- microbiology : Arabidopsis, Plant Diseases.
- physiology : Phytophthora, Pseudomonas syringae.
- Amino Acid Sequence, Molecular Sequence Data.
Abstract
The Arabidopsis pad2-1 mutant belongs to a series of non-allelic camalexin-deficient mutants. It was originally described as showing enhanced susceptibility to virulent strains of Pseudomonas syringae and was later shown to be hyper-susceptible to the oomycete pathogen Phytophthora brassicae (formerly P. porri). Surprisingly, in both pathosystems, the disease susceptibility of pad2-1 was not caused by the camalexin deficiency, suggesting additional roles of PAD2 in disease resistance. The susceptibility of pad2-1 to P. brassicae was used to map the mutation to the gene At4g23100, which encodes gamma-glutamylcysteine synthetase (gamma-ECS, GSH1). GSH1 catalyzes the first committed step of glutathione (GSH) biosynthesis. The pad2-1 mutation caused an S to N transition at amino acid position 298 close to the active center. The conclusion that PAD2 encodes GSH1 is supported by several lines of evidence: (i) pad2-1 mutants contained only about 22% of wild-type amounts of GSH, (ii) genetic complementation of pad2-1 with wild-type GSH1 cDNA restored GSH production, accumulation of camalexin in response to P. syringae and resistance to P. brassicae and P. syringae, (iii) another GSH1 mutant, cad2-1, showed pad2-like phenotypes, and (iv) feeding of GSH to excised leaves of pad2-1 restored camalexin production and resistance to P. brassicae. Inoculation of Col-0 with P. brassicae caused a coordinated increase in the transcript abundance of GSH1 and GSH2, the gene encoding the second enzyme in GSH biosynthesis, and resulted in enhanced foliar GSH accumulation. The pad2-1 mutant showed enhanced susceptibility to additional pathogens, suggesting an important general role of GSH in disease resistance of Arabidopsis.
DOI: 10.1111/j.1365-313X.2006.02938.x
PubMed: 17144898
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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It was originally described as showing enhanced susceptibility to virulent strains of Pseudomonas syringae and was later shown to be hyper-susceptible to the oomycete pathogen Phytophthora brassicae (formerly P. porri). Surprisingly, in both pathosystems, the disease susceptibility of pad2-1 was not caused by the camalexin deficiency, suggesting additional roles of PAD2 in disease resistance. The susceptibility of pad2-1 to P. brassicae was used to map the mutation to the gene At4g23100, which encodes gamma-glutamylcysteine synthetase (gamma-ECS, GSH1). GSH1 catalyzes the first committed step of glutathione (GSH) biosynthesis. The pad2-1 mutation caused an S to N transition at amino acid position 298 close to the active center. The conclusion that PAD2 encodes GSH1 is supported by several lines of evidence: (i) pad2-1 mutants contained only about 22% of wild-type amounts of GSH, (ii) genetic complementation of pad2-1 with wild-type GSH1 cDNA restored GSH production, accumulation of camalexin in response to P. syringae and resistance to P. brassicae and P. syringae, (iii) another GSH1 mutant, cad2-1, showed pad2-like phenotypes, and (iv) feeding of GSH to excised leaves of pad2-1 restored camalexin production and resistance to P. brassicae. Inoculation of Col-0 with P. brassicae caused a coordinated increase in the transcript abundance of GSH1 and GSH2, the gene encoding the second enzyme in GSH biosynthesis, and resulted in enhanced foliar GSH accumulation. The pad2-1 mutant showed enhanced susceptibility to additional pathogens, suggesting an important general role of GSH in disease resistance of Arabidopsis.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17144898</PMID><DateCompleted><Year>2007</Year><Month>04</Month><Day>06</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0960-7412</ISSN><JournalIssue CitedMedium="Print"><Volume>49</Volume><Issue>1</Issue><PubDate><Year>2007</Year><Month>Jan</Month></PubDate></JournalIssue><Title>The Plant journal : for cell and molecular biology</Title><ISOAbbreviation>Plant J</ISOAbbreviation></Journal><ArticleTitle>Identification of PAD2 as a gamma-glutamylcysteine synthetase highlights the importance of glutathione in disease resistance of Arabidopsis.</ArticleTitle><Pagination><MedlinePgn>159-72</MedlinePgn></Pagination><Abstract><AbstractText>The Arabidopsis pad2-1 mutant belongs to a series of non-allelic camalexin-deficient mutants. It was originally described as showing enhanced susceptibility to virulent strains of Pseudomonas syringae and was later shown to be hyper-susceptible to the oomycete pathogen Phytophthora brassicae (formerly P. porri). Surprisingly, in both pathosystems, the disease susceptibility of pad2-1 was not caused by the camalexin deficiency, suggesting additional roles of PAD2 in disease resistance. The susceptibility of pad2-1 to P. brassicae was used to map the mutation to the gene At4g23100, which encodes gamma-glutamylcysteine synthetase (gamma-ECS, GSH1). GSH1 catalyzes the first committed step of glutathione (GSH) biosynthesis. The pad2-1 mutation caused an S to N transition at amino acid position 298 close to the active center. The conclusion that PAD2 encodes GSH1 is supported by several lines of evidence: (i) pad2-1 mutants contained only about 22% of wild-type amounts of GSH, (ii) genetic complementation of pad2-1 with wild-type GSH1 cDNA restored GSH production, accumulation of camalexin in response to P. syringae and resistance to P. brassicae and P. syringae, (iii) another GSH1 mutant, cad2-1, showed pad2-like phenotypes, and (iv) feeding of GSH to excised leaves of pad2-1 restored camalexin production and resistance to P. brassicae. Inoculation of Col-0 with P. brassicae caused a coordinated increase in the transcript abundance of GSH1 and GSH2, the gene encoding the second enzyme in GSH biosynthesis, and resulted in enhanced foliar GSH accumulation. The pad2-1 mutant showed enhanced susceptibility to additional pathogens, suggesting an important general role of GSH in disease resistance of Arabidopsis.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Parisy</LastName><ForeName>Vincent</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Department of Biology, University of Fribourg, Fribourg, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Poinssot</LastName><ForeName>Benoit</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Owsianowski</LastName><ForeName>Lucas</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Buchala</LastName><ForeName>Antony</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Glazebrook</LastName><ForeName>Jane</ForeName><Initials>J</Initials></Author><Author 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PubStatus="entrez"><Year>2006</Year><Month>12</Month><Day>6</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17144898</ArticleId><ArticleId IdType="pii">TPJ2938</ArticleId><ArticleId IdType="doi">10.1111/j.1365-313X.2006.02938.x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suisse</li></country><region><li>Canton de Fribourg</li></region><settlement><li>Fribourg</li></settlement><orgName><li>Université de Fribourg</li></orgName></list><tree><noCountry><name sortKey="Buchala, Antony" sort="Buchala, Antony" uniqKey="Buchala A" first="Antony" last="Buchala">Antony Buchala</name><name sortKey="Glazebrook, Jane" sort="Glazebrook, Jane" uniqKey="Glazebrook J" first="Jane" last="Glazebrook">Jane Glazebrook</name><name sortKey="Mauch, Felix" sort="Mauch, Felix" uniqKey="Mauch F" first="Felix" last="Mauch">Felix Mauch</name><name sortKey="Owsianowski, Lucas" sort="Owsianowski, Lucas" uniqKey="Owsianowski L" first="Lucas" last="Owsianowski">Lucas Owsianowski</name><name sortKey="Poinssot, Benoit" sort="Poinssot, Benoit" uniqKey="Poinssot B" first="Benoit" last="Poinssot">Benoit Poinssot</name></noCountry><country name="Suisse"><region name="Canton de Fribourg"><name sortKey="Parisy, Vincent" sort="Parisy, Vincent" uniqKey="Parisy V" first="Vincent" last="Parisy">Vincent Parisy</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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