Accumulation of metal-binding peptides in fission yeast requires hmt2+.
Identifieur interne : 000413 ( Main/Corpus ); précédent : 000412; suivant : 000414Accumulation of metal-binding peptides in fission yeast requires hmt2+.
Auteurs : J G Vande Weghe ; D W OwSource :
- Molecular microbiology [ 0950-382X ] ; 2001.
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
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pubmed:11679064Le 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><nlm:affiliation>Plant Gene Expression Center, U.S. Department of Agriculture-Agricultural Research Service, 800 Buchanan Street, Albany, CA 94710, USA.</nlm:affiliation></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></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><nlm:affiliation>Plant Gene Expression Center, U.S. Department of Agriculture-Agricultural Research Service, 800 Buchanan Street, Albany, CA 94710, USA.</nlm:affiliation></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="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="cytology" xml:lang="en"><term>Schizosaccharomyces</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="metabolism" xml:lang="en"><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Microscopy, Fluorescence</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 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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" 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