Accumulation of metal-binding peptides in fission yeast requires hmt2+.
Identifieur interne : 000421 ( Main/Exploration ); précédent : 000420; suivant : 000422Accumulation of metal-binding peptides in fission yeast requires hmt2+.
Auteurs : J G Vande Weghe [États-Unis] ; D W OwSource :
- Molecular microbiology [ 0950-382X ] ; 2001.
Descripteurs français
- KwdFr :
- Aminoacyltransferases (antagonistes et inhibiteurs), Aminoacyltransferases (métabolisme), Cadmium (métabolisme), Chélateurs (métabolisme), Cytochromes de type c (génétique), Cytochromes de type c (métabolisme), Glutathion (MeSH), Microscopie de fluorescence (MeSH), Mitochondries (enzymologie), Métalloprotéines (métabolisme), Métaux lourds (métabolisme), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Phytochélatines (MeSH), Protéines de Schizosaccharomyces pombe (métabolisme), Radio-isotopes du soufre (métabolisme), Schizosaccharomyces (cytologie), Schizosaccharomyces (génétique), Schizosaccharomyces (métabolisme), Sulfures (métabolisme).
- MESH :
- antagonistes et inhibiteurs : Aminoacyltransferases.
- cytologie : Schizosaccharomyces.
- enzymologie : Mitochondries.
- génétique : Cytochromes de type c, Oxidoreductases, Schizosaccharomyces.
- métabolisme : Aminoacyltransferases, Cadmium, Chélateurs, Cytochromes de type c, Métalloprotéines, Métaux lourds, Oxidoreductases, Protéines de Schizosaccharomyces pombe, Radio-isotopes du soufre, Schizosaccharomyces, Sulfures.
- Glutathion, Microscopie de fluorescence, Phytochélatines.
English descriptors
- KwdEn :
- Aminoacyltransferases (antagonists & inhibitors), Aminoacyltransferases (metabolism), Cadmium (metabolism), Chelating Agents (metabolism), Cytochrome c Group (genetics), Cytochrome c Group (metabolism), Glutathione (MeSH), Metalloproteins (metabolism), Metals, Heavy (metabolism), Microscopy, Fluorescence (MeSH), Mitochondria (enzymology), Oxidoreductases (genetics), Oxidoreductases (metabolism), Phytochelatins (MeSH), Schizosaccharomyces (cytology), Schizosaccharomyces (genetics), Schizosaccharomyces (metabolism), Schizosaccharomyces pombe Proteins (metabolism), Sulfides (metabolism), Sulfur Radioisotopes (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Aminoacyltransferases.
- chemical , genetics : Cytochrome c Group, Oxidoreductases.
- chemical , metabolism : Aminoacyltransferases, Cadmium, Chelating Agents, Cytochrome c Group, Metalloproteins, Metals, Heavy, Oxidoreductases, Schizosaccharomyces pombe Proteins, Sulfides, Sulfur Radioisotopes.
- chemical : Glutathione, Phytochelatins.
- cytology : Schizosaccharomyces.
- enzymology : Mitochondria.
- genetics : Schizosaccharomyces.
- metabolism : Schizosaccharomyces.
- Microscopy, Fluorescence.
Abstract
The fission yeast Schizosaccharomyces pombe detoxifies cadmium by synthesizing phytochelatins, peptides of the structure (gamma-GluCys)nGly, which bind cadmium and mediate its sequestration into the vacuole. The fission yeast protein HMT2, a mitochondrial enzyme that can oxidize sulphide, appears to be essential for tolerance to multiple forms of stress, including exposure to cadmium. We found that the hmt2- mutant is unable to accumulate normal levels of phytochelatins in response to cadmium, although the cells possess a phytochelatin synthase that is active in vitro. Radioactive pulse-chase experiments demonstrated that the defect lies in two steps: the synthesis of phytochelations and the upregulation of glutathione production. Phytochelatins, once formed, are stable. hmt2- cells accumulate high levels of sulphide and, when exposed to cadmium, display bright fluorescent bodies consistent with cadmium sulphide. We propose that the precipitation of free cadmium blocks phytochelatin synthesis in vivo, by preventing upregulation of glutathione production and formation of the cadmium-glutathione thiolate required as a substrate by phytochelatin synthase. Thus, although sulphide is required for phytochelatin-mediated metal tolerance, aberrantly high sulphide levels can inhibit this pathway. Precise regulation of sulphur metabolism, mediated in part by HMT2, is essential for metal tolerance in fission yeast.
DOI: 10.1046/j.1365-2958.2001.02624.x
PubMed: 11679064
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Accumulation of metal-binding peptides in fission yeast requires hmt2+.</title>
<author><name sortKey="Vande Weghe, J G" sort="Vande Weghe, J G" uniqKey="Vande Weghe J" first="J G" last="Vande Weghe">J G Vande Weghe</name>
<affiliation wicri:level="2"><nlm:affiliation>Plant Gene Expression Center, U.S. Department of Agriculture-Agricultural Research Service, 800 Buchanan Street, Albany, CA 94710, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Plant Gene Expression Center, U.S. Department of Agriculture-Agricultural Research Service, 800 Buchanan Street, Albany, CA 94710</wicri:regionArea>
<placeName><region type="state">Californie</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Ow, D W" sort="Ow, D W" uniqKey="Ow D" first="D W" last="Ow">D W Ow</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2001">2001</date>
<idno type="RBID">pubmed:11679064</idno>
<idno type="pmid">11679064</idno>
<idno type="doi">10.1046/j.1365-2958.2001.02624.x</idno>
<idno type="wicri:Area/Main/Corpus">000413</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000413</idno>
<idno type="wicri:Area/Main/Curation">000413</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000413</idno>
<idno type="wicri:Area/Main/Exploration">000413</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Accumulation of metal-binding peptides in fission yeast requires hmt2+.</title>
<author><name sortKey="Vande Weghe, J G" sort="Vande Weghe, J G" uniqKey="Vande Weghe J" first="J G" last="Vande Weghe">J G Vande Weghe</name>
<affiliation wicri:level="2"><nlm:affiliation>Plant Gene Expression Center, U.S. Department of Agriculture-Agricultural Research Service, 800 Buchanan Street, Albany, CA 94710, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Plant Gene Expression Center, U.S. Department of Agriculture-Agricultural Research Service, 800 Buchanan Street, Albany, CA 94710</wicri:regionArea>
<placeName><region type="state">Californie</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Ow, D W" sort="Ow, D W" uniqKey="Ow D" first="D W" last="Ow">D W Ow</name>
</author>
</analytic>
<series><title level="j">Molecular microbiology</title>
<idno type="ISSN">0950-382X</idno>
<imprint><date when="2001" type="published">2001</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aminoacyltransferases (antagonists & inhibitors)</term>
<term>Aminoacyltransferases (metabolism)</term>
<term>Cadmium (metabolism)</term>
<term>Chelating Agents (metabolism)</term>
<term>Cytochrome c Group (genetics)</term>
<term>Cytochrome c Group (metabolism)</term>
<term>Glutathione (MeSH)</term>
<term>Metalloproteins (metabolism)</term>
<term>Metals, Heavy (metabolism)</term>
<term>Microscopy, Fluorescence (MeSH)</term>
<term>Mitochondria (enzymology)</term>
<term>Oxidoreductases (genetics)</term>
<term>Oxidoreductases (metabolism)</term>
<term>Phytochelatins (MeSH)</term>
<term>Schizosaccharomyces (cytology)</term>
<term>Schizosaccharomyces (genetics)</term>
<term>Schizosaccharomyces (metabolism)</term>
<term>Schizosaccharomyces pombe Proteins (metabolism)</term>
<term>Sulfides (metabolism)</term>
<term>Sulfur Radioisotopes (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Aminoacyltransferases (antagonistes et inhibiteurs)</term>
<term>Aminoacyltransferases (métabolisme)</term>
<term>Cadmium (métabolisme)</term>
<term>Chélateurs (métabolisme)</term>
<term>Cytochromes de type c (génétique)</term>
<term>Cytochromes de type c (métabolisme)</term>
<term>Glutathion (MeSH)</term>
<term>Microscopie de fluorescence (MeSH)</term>
<term>Mitochondries (enzymologie)</term>
<term>Métalloprotéines (métabolisme)</term>
<term>Métaux lourds (métabolisme)</term>
<term>Oxidoreductases (génétique)</term>
<term>Oxidoreductases (métabolisme)</term>
<term>Phytochélatines (MeSH)</term>
<term>Protéines de Schizosaccharomyces pombe (métabolisme)</term>
<term>Radio-isotopes du soufre (métabolisme)</term>
<term>Schizosaccharomyces (cytologie)</term>
<term>Schizosaccharomyces (génétique)</term>
<term>Schizosaccharomyces (métabolisme)</term>
<term>Sulfures (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Aminoacyltransferases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cytochrome c Group</term>
<term>Oxidoreductases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Aminoacyltransferases</term>
<term>Cadmium</term>
<term>Chelating Agents</term>
<term>Cytochrome c Group</term>
<term>Metalloproteins</term>
<term>Metals, Heavy</term>
<term>Oxidoreductases</term>
<term>Schizosaccharomyces pombe Proteins</term>
<term>Sulfides</term>
<term>Sulfur Radioisotopes</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Glutathione</term>
<term>Phytochelatins</term>
</keywords>
<keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Aminoacyltransferases</term>
</keywords>
<keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Schizosaccharomyces</term>
</keywords>
<keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Schizosaccharomyces</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Mitochondries</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Mitochondria</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Schizosaccharomyces</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Cytochromes de type c</term>
<term>Oxidoreductases</term>
<term>Schizosaccharomyces</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Schizosaccharomyces</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Aminoacyltransferases</term>
<term>Cadmium</term>
<term>Chélateurs</term>
<term>Cytochromes de type c</term>
<term>Métalloprotéines</term>
<term>Métaux lourds</term>
<term>Oxidoreductases</term>
<term>Protéines de Schizosaccharomyces pombe</term>
<term>Radio-isotopes du soufre</term>
<term>Schizosaccharomyces</term>
<term>Sulfures</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Microscopy, Fluorescence</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Glutathion</term>
<term>Microscopie de fluorescence</term>
<term>Phytochélatines</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">The fission yeast Schizosaccharomyces pombe detoxifies cadmium by synthesizing phytochelatins, peptides of the structure (gamma-GluCys)nGly, which bind cadmium and mediate its sequestration into the vacuole. The fission yeast protein HMT2, a mitochondrial enzyme that can oxidize sulphide, appears to be essential for tolerance to multiple forms of stress, including exposure to cadmium. We found that the hmt2- mutant is unable to accumulate normal levels of phytochelatins in response to cadmium, although the cells possess a phytochelatin synthase that is active in vitro. Radioactive pulse-chase experiments demonstrated that the defect lies in two steps: the synthesis of phytochelations and the upregulation of glutathione production. Phytochelatins, once formed, are stable. hmt2- cells accumulate high levels of sulphide and, when exposed to cadmium, display bright fluorescent bodies consistent with cadmium sulphide. We propose that the precipitation of free cadmium blocks phytochelatin synthesis in vivo, by preventing upregulation of glutathione production and formation of the cadmium-glutathione thiolate required as a substrate by phytochelatin synthase. Thus, although sulphide is required for phytochelatin-mediated metal tolerance, aberrantly high sulphide levels can inhibit this pathway. Precise regulation of sulphur metabolism, mediated in part by HMT2, is essential for metal tolerance in fission yeast.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11679064</PMID>
<DateCompleted><Year>2002</Year>
<Month>01</Month>
<Day>31</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>07</Month>
<Day>25</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Print">0950-382X</ISSN>
<JournalIssue CitedMedium="Print"><Volume>42</Volume>
<Issue>1</Issue>
<PubDate><Year>2001</Year>
<Month>Oct</Month>
</PubDate>
</JournalIssue>
<Title>Molecular microbiology</Title>
<ISOAbbreviation>Mol Microbiol</ISOAbbreviation>
</Journal>
<ArticleTitle>Accumulation of metal-binding peptides in fission yeast requires hmt2+.</ArticleTitle>
<Pagination><MedlinePgn>29-36</MedlinePgn>
</Pagination>
<Abstract><AbstractText>The fission yeast Schizosaccharomyces pombe detoxifies cadmium by synthesizing phytochelatins, peptides of the structure (gamma-GluCys)nGly, which bind cadmium and mediate its sequestration into the vacuole. The fission yeast protein HMT2, a mitochondrial enzyme that can oxidize sulphide, appears to be essential for tolerance to multiple forms of stress, including exposure to cadmium. We found that the hmt2- mutant is unable to accumulate normal levels of phytochelatins in response to cadmium, although the cells possess a phytochelatin synthase that is active in vitro. Radioactive pulse-chase experiments demonstrated that the defect lies in two steps: the synthesis of phytochelations and the upregulation of glutathione production. Phytochelatins, once formed, are stable. hmt2- cells accumulate high levels of sulphide and, when exposed to cadmium, display bright fluorescent bodies consistent with cadmium sulphide. We propose that the precipitation of free cadmium blocks phytochelatin synthesis in vivo, by preventing upregulation of glutathione production and formation of the cadmium-glutathione thiolate required as a substrate by phytochelatin synthase. Thus, although sulphide is required for phytochelatin-mediated metal tolerance, aberrantly high sulphide levels can inhibit this pathway. Precise regulation of sulphur metabolism, mediated in part by HMT2, is essential for metal tolerance in fission yeast.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Vande Weghe</LastName>
<ForeName>J G</ForeName>
<Initials>JG</Initials>
<AffiliationInfo><Affiliation>Plant Gene Expression Center, U.S. Department of Agriculture-Agricultural Research Service, 800 Buchanan Street, Albany, CA 94710, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ow</LastName>
<ForeName>D W</ForeName>
<Initials>DW</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType>
</PublicationTypeList>
</Article>
<MedlineJournalInfo><Country>England</Country>
<MedlineTA>Mol Microbiol</MedlineTA>
<NlmUniqueID>8712028</NlmUniqueID>
<ISSNLinking>0950-382X</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D002614">Chelating Agents</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D003574">Cytochrome c Group</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D008667">Metalloproteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D019216">Metals, Heavy</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D029702">Schizosaccharomyces pombe Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D013440">Sulfides</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D013462">Sulfur Radioisotopes</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>00BH33GNGH</RegistryNumber>
<NameOfSubstance UI="D002104">Cadmium</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>98726-08-0</RegistryNumber>
<NameOfSubstance UI="D054811">Phytochelatins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.-</RegistryNumber>
<NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.8.2.-</RegistryNumber>
<NameOfSubstance UI="C064500">flavocytochrome c sulfide dehydrogenase</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.3.2.-</RegistryNumber>
<NameOfSubstance UI="D019881">Aminoacyltransferases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.3.2.15</RegistryNumber>
<NameOfSubstance UI="C093784">glutathione gamma-glutamylcysteinyltransferase</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber>
<NameOfSubstance UI="D005978">Glutathione</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D019881" MajorTopicYN="N">Aminoacyltransferases</DescriptorName>
<QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002104" MajorTopicYN="N">Cadmium</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002614" MajorTopicYN="N">Chelating Agents</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003574" MajorTopicYN="N">Cytochrome c Group</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008667" MajorTopicYN="N">Metalloproteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D019216" MajorTopicYN="N">Metals, Heavy</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008856" MajorTopicYN="N">Microscopy, Fluorescence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008928" MajorTopicYN="N">Mitochondria</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D054811" MajorTopicYN="N">Phytochelatins</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012568" MajorTopicYN="N">Schizosaccharomyces</DescriptorName>
<QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D029702" MajorTopicYN="N">Schizosaccharomyces pombe Proteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013440" MajorTopicYN="N">Sulfides</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013462" MajorTopicYN="N">Sulfur Radioisotopes</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2001</Year>
<Month>10</Month>
<Day>27</Day>
<Hour>10</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2002</Year>
<Month>2</Month>
<Day>1</Day>
<Hour>10</Hour>
<Minute>1</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2001</Year>
<Month>10</Month>
<Day>27</Day>
<Hour>10</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">11679064</ArticleId>
<ArticleId IdType="pii">2624</ArticleId>
<ArticleId IdType="doi">10.1046/j.1365-2958.2001.02624.x</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>États-Unis</li>
</country>
<region><li>Californie</li>
</region>
</list>
<tree><noCountry><name sortKey="Ow, D W" sort="Ow, D W" uniqKey="Ow D" first="D W" last="Ow">D W Ow</name>
</noCountry>
<country name="États-Unis"><region name="Californie"><name sortKey="Vande Weghe, J G" sort="Vande Weghe, J G" uniqKey="Vande Weghe J" first="J G" last="Vande Weghe">J G Vande Weghe</name>
</region>
</country>
</tree>
</affiliations>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/MetalBindProtPlantV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000421 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000421 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Bois |area= MetalBindProtPlantV1 |flux= Main |étape= Exploration |type= RBID |clé= pubmed:11679064 |texte= Accumulation of metal-binding peptides in fission yeast requires hmt2+. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:11679064" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \ | NlmPubMed2Wicri -a MetalBindProtPlantV1
This area was generated with Dilib version V0.6.38. |