Drosophila ABC transporter, DmHMT-1, confers tolerance to cadmium. DmHMT-1 and its yeast homolog, SpHMT-1, are not essential for vacuolar phytochelatin sequestration.
Identifieur interne : 001F86 ( Main/Exploration ); précédent : 001F85; suivant : 001F87Drosophila ABC transporter, DmHMT-1, confers tolerance to cadmium. DmHMT-1 and its yeast homolog, SpHMT-1, are not essential for vacuolar phytochelatin sequestration.
Auteurs : Thanwalee Sooksa-Nguan [États-Unis] ; Bakhtiyor Yakubov ; Volodymyr I. Kozlovskyy ; Caitlin M. Barkume ; Kevin J. Howe ; Theodore W. Thannhauser ; Michael A. Rutzke ; Jonathan J. Hart ; Leon V. Kochian ; Philip A. Rea ; Olena K. VatamaniukSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2009.
Descripteurs français
- KwdFr :
- Aminoacyltransferases (génétique), Aminoacyltransferases (métabolisme), Animaux (MeSH), Cadmium (pharmacologie), Caenorhabditis elegans (génétique), Caenorhabditis elegans (métabolisme), Chlamydomonas reinhardtii (génétique), Chlamydomonas reinhardtii (métabolisme), Données de séquences moléculaires (MeSH), Drosophila (MeSH), Phytochélatines (génétique), Phytochélatines (métabolisme), Protéines de Drosophila (génétique), Protéines de Drosophila (métabolisme), Résistance des champignons aux médicaments (effets des médicaments et des substances chimiques), Résistance des champignons aux médicaments (physiologie), Schizosaccharomyces (génétique), Schizosaccharomyces (métabolisme), Séquence nucléotidique (MeSH), Test de complémentation (MeSH), Transport biologique (effets des médicaments et des substances chimiques), Transport biologique (physiologie), Transporteurs ABC (génétique), Transporteurs ABC (métabolisme), Vacuoles (génétique), Vacuoles (métabolisme).
- MESH :
- effets des médicaments et des substances chimiques : Résistance des champignons aux médicaments, Transport biologique.
- génétique : Aminoacyltransferases, Caenorhabditis elegans, Chlamydomonas reinhardtii, Phytochélatines, Protéines de Drosophila, Schizosaccharomyces, Transporteurs ABC, Vacuoles.
- métabolisme : Aminoacyltransferases, Caenorhabditis elegans, Chlamydomonas reinhardtii, Phytochélatines, Protéines de Drosophila, Schizosaccharomyces, Transporteurs ABC, Vacuoles.
- pharmacologie : Cadmium.
- physiologie : Résistance des champignons aux médicaments, Transport biologique.
- Animaux, Données de séquences moléculaires, Drosophila, Séquence nucléotidique, Test de complémentation.
English descriptors
- KwdEn :
- ATP-Binding Cassette Transporters (genetics), ATP-Binding Cassette Transporters (metabolism), Aminoacyltransferases (genetics), Aminoacyltransferases (metabolism), Animals (MeSH), Base Sequence (MeSH), Biological Transport (drug effects), Biological Transport (physiology), Cadmium (pharmacology), Caenorhabditis elegans (genetics), Caenorhabditis elegans (metabolism), Chlamydomonas reinhardtii (genetics), Chlamydomonas reinhardtii (metabolism), Drosophila (MeSH), Drosophila Proteins (genetics), Drosophila Proteins (metabolism), Drug Resistance, Fungal (drug effects), Drug Resistance, Fungal (physiology), Genetic Complementation Test (MeSH), Molecular Sequence Data (MeSH), Phytochelatins (genetics), Phytochelatins (metabolism), Schizosaccharomyces (genetics), Schizosaccharomyces (metabolism), Vacuoles (genetics), Vacuoles (metabolism).
- MESH :
- chemical , genetics : ATP-Binding Cassette Transporters, Aminoacyltransferases, Drosophila Proteins, Phytochelatins.
- chemical , metabolism : ATP-Binding Cassette Transporters, Aminoacyltransferases, Drosophila Proteins, Phytochelatins.
- drug effects : Biological Transport, Drug Resistance, Fungal.
- genetics : Caenorhabditis elegans, Chlamydomonas reinhardtii, Schizosaccharomyces, Vacuoles.
- metabolism : Caenorhabditis elegans, Chlamydomonas reinhardtii, Schizosaccharomyces, Vacuoles.
- chemical , pharmacology : Cadmium.
- physiology : Biological Transport, Drug Resistance, Fungal.
- Animals, Base Sequence, Drosophila, Genetic Complementation Test, Molecular Sequence Data.
Abstract
Half-molecule ATP-binding cassette transporters of the HMT-1 (heavy metal tolerance factor 1) subfamily are required for Cd2+ tolerance in Schizosaccharomyces pombe, Caenorhabditis elegans, and Chlamydomonas reinhardtii. Based on studies of S. pombe, it has been proposed that SpHMT-1 transports heavy metal.phytochelatin (PC) complexes into the vacuolysosomal compartment. PCs are glutathione derivatives synthesized by PC synthases (PCS) in plants, fungi, and C. elegans in response to heavy metals. Our previous studies in C. elegans, however, suggested that HMT-1 and PCS-1 do not necessarily act in concert in metal detoxification. To further explore this inconsistency, we have gone on to test whether DmHMT-1, an HMT-1 from a new source, Drosophila, whose genome lacks PCS homologs, functions in heavy metal detoxification. In so doing, we show that heterologously expressed DmHMT-1 suppresses the Cd2+ hypersensitivity of S. pombe hmt-1 mutants and localizes to the vacuolar membrane but does not transport Cd.PC complexes. Crucially, similar analyses of S. pombe hmt-1 mutants extend this finding to show that SpHMT-1 itself either does not transport Cd.PC complexes or is not the principal Cd.PC/apoPC transporter. Consistent with this discovery and with our previous suggestion that HMT-1 and PCS-1 do not operate in a simple linear metal detoxification pathway, we demonstrate that, unlike PCS-deficient cells, which are hypersensitive to several heavy metals, SpHMT-1-deficient cells are hypersensitive to Cd2+, but not to Hg2+ or As3+. These findings significantly change our current understanding of the function of HMT-1 proteins and invoke a PC-independent role for these transporters in Cd2+ detoxification.
DOI: 10.1074/jbc.M806501200
PubMed: 19001374
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Kochian</name></author><author><name sortKey="Rea, Philip A" sort="Rea, Philip A" uniqKey="Rea P" first="Philip A" last="Rea">Philip A. Rea</name></author><author><name sortKey="Vatamaniuk, Olena K" sort="Vatamaniuk, Olena K" uniqKey="Vatamaniuk O" first="Olena K" last="Vatamaniuk">Olena K. Vatamaniuk</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>ATP-Binding Cassette Transporters (genetics)</term><term>ATP-Binding Cassette Transporters (metabolism)</term><term>Aminoacyltransferases (genetics)</term><term>Aminoacyltransferases (metabolism)</term><term>Animals (MeSH)</term><term>Base Sequence (MeSH)</term><term>Biological Transport (drug effects)</term><term>Biological Transport (physiology)</term><term>Cadmium (pharmacology)</term><term>Caenorhabditis elegans (genetics)</term><term>Caenorhabditis elegans (metabolism)</term><term>Chlamydomonas reinhardtii (genetics)</term><term>Chlamydomonas reinhardtii (metabolism)</term><term>Drosophila (MeSH)</term><term>Drosophila Proteins (genetics)</term><term>Drosophila Proteins (metabolism)</term><term>Drug Resistance, Fungal (drug effects)</term><term>Drug Resistance, Fungal (physiology)</term><term>Genetic Complementation Test (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Phytochelatins (genetics)</term><term>Phytochelatins (metabolism)</term><term>Schizosaccharomyces (genetics)</term><term>Schizosaccharomyces (metabolism)</term><term>Vacuoles (genetics)</term><term>Vacuoles (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Aminoacyltransferases (génétique)</term><term>Aminoacyltransferases (métabolisme)</term><term>Animaux (MeSH)</term><term>Cadmium (pharmacologie)</term><term>Caenorhabditis elegans (génétique)</term><term>Caenorhabditis elegans (métabolisme)</term><term>Chlamydomonas reinhardtii (génétique)</term><term>Chlamydomonas reinhardtii (métabolisme)</term><term>Données de séquences moléculaires (MeSH)</term><term>Drosophila (MeSH)</term><term>Phytochélatines (génétique)</term><term>Phytochélatines (métabolisme)</term><term>Protéines de Drosophila (génétique)</term><term>Protéines de Drosophila (métabolisme)</term><term>Résistance des champignons aux médicaments (effets des médicaments et des substances chimiques)</term><term>Résistance des champignons aux médicaments (physiologie)</term><term>Schizosaccharomyces (génétique)</term><term>Schizosaccharomyces (métabolisme)</term><term>Séquence nucléotidique (MeSH)</term><term>Test de complémentation (MeSH)</term><term>Transport biologique (effets des médicaments et des substances chimiques)</term><term>Transport biologique (physiologie)</term><term>Transporteurs ABC (génétique)</term><term>Transporteurs ABC (métabolisme)</term><term>Vacuoles (génétique)</term><term>Vacuoles (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>ATP-Binding Cassette Transporters</term><term>Aminoacyltransferases</term><term>Drosophila Proteins</term><term>Phytochelatins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>ATP-Binding Cassette Transporters</term><term>Aminoacyltransferases</term><term>Drosophila Proteins</term><term>Phytochelatins</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Biological Transport</term><term>Drug Resistance, Fungal</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Résistance des champignons aux médicaments</term><term>Transport biologique</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Caenorhabditis elegans</term><term>Chlamydomonas reinhardtii</term><term>Schizosaccharomyces</term><term>Vacuoles</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Aminoacyltransferases</term><term>Caenorhabditis elegans</term><term>Chlamydomonas reinhardtii</term><term>Phytochélatines</term><term>Protéines de Drosophila</term><term>Schizosaccharomyces</term><term>Transporteurs ABC</term><term>Vacuoles</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Caenorhabditis elegans</term><term>Chlamydomonas reinhardtii</term><term>Schizosaccharomyces</term><term>Vacuoles</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Aminoacyltransferases</term><term>Caenorhabditis elegans</term><term>Chlamydomonas reinhardtii</term><term>Phytochélatines</term><term>Protéines de Drosophila</term><term>Schizosaccharomyces</term><term>Transporteurs ABC</term><term>Vacuoles</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Cadmium</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Cadmium</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Résistance des champignons aux médicaments</term><term>Transport biologique</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Biological Transport</term><term>Drug Resistance, Fungal</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Base Sequence</term><term>Drosophila</term><term>Genetic Complementation Test</term><term>Molecular Sequence Data</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Données de séquences moléculaires</term><term>Drosophila</term><term>Séquence nucléotidique</term><term>Test de complémentation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Half-molecule ATP-binding cassette transporters of the HMT-1 (heavy metal tolerance factor 1) subfamily are required for Cd2+ tolerance in Schizosaccharomyces pombe, Caenorhabditis elegans, and Chlamydomonas reinhardtii. Based on studies of S. pombe, it has been proposed that SpHMT-1 transports heavy metal.phytochelatin (PC) complexes into the vacuolysosomal compartment. PCs are glutathione derivatives synthesized by PC synthases (PCS) in plants, fungi, and C. elegans in response to heavy metals. Our previous studies in C. elegans, however, suggested that HMT-1 and PCS-1 do not necessarily act in concert in metal detoxification. To further explore this inconsistency, we have gone on to test whether DmHMT-1, an HMT-1 from a new source, Drosophila, whose genome lacks PCS homologs, functions in heavy metal detoxification. In so doing, we show that heterologously expressed DmHMT-1 suppresses the Cd2+ hypersensitivity of S. pombe hmt-1 mutants and localizes to the vacuolar membrane but does not transport Cd.PC complexes. Crucially, similar analyses of S. pombe hmt-1 mutants extend this finding to show that SpHMT-1 itself either does not transport Cd.PC complexes or is not the principal Cd.PC/apoPC transporter. Consistent with this discovery and with our previous suggestion that HMT-1 and PCS-1 do not operate in a simple linear metal detoxification pathway, we demonstrate that, unlike PCS-deficient cells, which are hypersensitive to several heavy metals, SpHMT-1-deficient cells are hypersensitive to Cd2+, but not to Hg2+ or As3+. These findings significantly change our current understanding of the function of HMT-1 proteins and invoke a PC-independent role for these transporters in Cd2+ detoxification.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19001374</PMID><DateCompleted><Year>2009</Year><Month>02</Month><Day>24</Day></DateCompleted><DateRevised><Year>2017</Year><Month>12</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>284</Volume><Issue>1</Issue><PubDate><Year>2009</Year><Month>Jan</Month><Day>02</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Drosophila ABC transporter, DmHMT-1, confers tolerance to cadmium. DmHMT-1 and its yeast homolog, SpHMT-1, are not essential for vacuolar phytochelatin sequestration.</ArticleTitle><Pagination><MedlinePgn>354-62</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M806501200</ELocationID><Abstract><AbstractText>Half-molecule ATP-binding cassette transporters of the HMT-1 (heavy metal tolerance factor 1) subfamily are required for Cd2+ tolerance in Schizosaccharomyces pombe, Caenorhabditis elegans, and Chlamydomonas reinhardtii. Based on studies of S. pombe, it has been proposed that SpHMT-1 transports heavy metal.phytochelatin (PC) complexes into the vacuolysosomal compartment. PCs are glutathione derivatives synthesized by PC synthases (PCS) in plants, fungi, and C. elegans in response to heavy metals. Our previous studies in C. elegans, however, suggested that HMT-1 and PCS-1 do not necessarily act in concert in metal detoxification. To further explore this inconsistency, we have gone on to test whether DmHMT-1, an HMT-1 from a new source, Drosophila, whose genome lacks PCS homologs, functions in heavy metal detoxification. In so doing, we show that heterologously expressed DmHMT-1 suppresses the Cd2+ hypersensitivity of S. pombe hmt-1 mutants and localizes to the vacuolar membrane but does not transport Cd.PC complexes. Crucially, similar analyses of S. pombe hmt-1 mutants extend this finding to show that SpHMT-1 itself either does not transport Cd.PC complexes or is not the principal Cd.PC/apoPC transporter. Consistent with this discovery and with our previous suggestion that HMT-1 and PCS-1 do not operate in a simple linear metal detoxification pathway, we demonstrate that, unlike PCS-deficient cells, which are hypersensitive to several heavy metals, SpHMT-1-deficient cells are hypersensitive to Cd2+, but not to Hg2+ or As3+. These findings significantly change our current understanding of the function of HMT-1 proteins and invoke a PC-independent role for these transporters in Cd2+ detoxification.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sooksa-Nguan</LastName><ForeName>Thanwalee</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Crop and Soil Sciences, Cornell University, Ithaca, New York 14853, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yakubov</LastName><ForeName>Bakhtiyor</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Kozlovskyy</LastName><ForeName>Volodymyr I</ForeName><Initials>VI</Initials></Author><Author ValidYN="Y"><LastName>Barkume</LastName><ForeName>Caitlin M</ForeName><Initials>CM</Initials></Author><Author ValidYN="Y"><LastName>Howe</LastName><ForeName>Kevin J</ForeName><Initials>KJ</Initials></Author><Author ValidYN="Y"><LastName>Thannhauser</LastName><ForeName>Theodore W</ForeName><Initials>TW</Initials></Author><Author ValidYN="Y"><LastName>Rutzke</LastName><ForeName>Michael A</ForeName><Initials>MA</Initials></Author><Author ValidYN="Y"><LastName>Hart</LastName><ForeName>Jonathan J</ForeName><Initials>JJ</Initials></Author><Author ValidYN="Y"><LastName>Kochian</LastName><ForeName>Leon V</ForeName><Initials>LV</Initials></Author><Author ValidYN="Y"><LastName>Rea</LastName><ForeName>Philip A</ForeName><Initials>PA</Initials></Author><Author ValidYN="Y"><LastName>Vatamaniuk</LastName><ForeName>Olena K</ForeName><Initials>OK</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>ACE60575</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2008</Year><Month>11</Month><Day>10</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018528">ATP-Binding Cassette Transporters</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029721">Drosophila Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C489670">hmt1 protein, S pombe</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 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></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D018528" MajorTopicYN="N">ATP-Binding Cassette Transporters</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019881" MajorTopicYN="N">Aminoacyltransferases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001692" MajorTopicYN="N">Biological Transport</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002104" MajorTopicYN="N">Cadmium</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017173" MajorTopicYN="N">Caenorhabditis elegans</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016825" MajorTopicYN="N">Chlamydomonas reinhardtii</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004330" MajorTopicYN="N">Drosophila</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D029721" MajorTopicYN="N">Drosophila Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D025141" MajorTopicYN="N">Drug Resistance, Fungal</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005816" MajorTopicYN="N">Genetic Complementation Test</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054811" MajorTopicYN="N">Phytochelatins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012568" MajorTopicYN="N">Schizosaccharomyces</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014617" MajorTopicYN="N">Vacuoles</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2008</Year><Month>11</Month><Day>13</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2009</Year><Month>2</Month><Day>25</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2008</Year><Month>11</Month><Day>13</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19001374</ArticleId><ArticleId IdType="pii">M806501200</ArticleId><ArticleId IdType="doi">10.1074/jbc.M806501200</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>État de New York</li></region><settlement><li>Ithaca (New York)</li></settlement><orgName><li>Université Cornell</li></orgName></list><tree><noCountry><name sortKey="Barkume, Caitlin M" sort="Barkume, Caitlin M" uniqKey="Barkume C" first="Caitlin M" last="Barkume">Caitlin M. Barkume</name><name sortKey="Hart, Jonathan J" sort="Hart, Jonathan J" uniqKey="Hart J" first="Jonathan J" last="Hart">Jonathan J. Hart</name><name sortKey="Howe, Kevin J" sort="Howe, Kevin J" uniqKey="Howe K" first="Kevin J" last="Howe">Kevin J. Howe</name><name sortKey="Kochian, Leon V" sort="Kochian, Leon V" uniqKey="Kochian L" first="Leon V" last="Kochian">Leon V. Kochian</name><name sortKey="Kozlovskyy, Volodymyr I" sort="Kozlovskyy, Volodymyr I" uniqKey="Kozlovskyy V" first="Volodymyr I" last="Kozlovskyy">Volodymyr I. Kozlovskyy</name><name sortKey="Rea, Philip A" sort="Rea, Philip A" uniqKey="Rea P" first="Philip A" last="Rea">Philip A. Rea</name><name sortKey="Rutzke, Michael A" sort="Rutzke, Michael A" uniqKey="Rutzke M" first="Michael A" last="Rutzke">Michael A. Rutzke</name><name sortKey="Thannhauser, Theodore W" sort="Thannhauser, Theodore W" uniqKey="Thannhauser T" first="Theodore W" last="Thannhauser">Theodore W. Thannhauser</name><name sortKey="Vatamaniuk, Olena K" sort="Vatamaniuk, Olena K" uniqKey="Vatamaniuk O" first="Olena K" last="Vatamaniuk">Olena K. Vatamaniuk</name><name sortKey="Yakubov, Bakhtiyor" sort="Yakubov, Bakhtiyor" uniqKey="Yakubov B" first="Bakhtiyor" last="Yakubov">Bakhtiyor Yakubov</name></noCountry><country name="États-Unis"><region name="État de New York"><name sortKey="Sooksa Nguan, Thanwalee" sort="Sooksa Nguan, Thanwalee" uniqKey="Sooksa Nguan T" first="Thanwalee" last="Sooksa-Nguan">Thanwalee Sooksa-Nguan</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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|texte= Drosophila ABC transporter, DmHMT-1, confers tolerance to cadmium. DmHMT-1 and its yeast homolog, SpHMT-1, are not essential for vacuolar phytochelatin sequestration.
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