A heavy metal-associated protein (AcHMA1) from the halophyte, Atriplex canescens (Pursh) Nutt., confers tolerance to iron and other abiotic stresses when expressed in Saccharomyces cerevisiae.
Identifieur interne : 000167 ( Main/Exploration ); précédent : 000166; suivant : 000168A heavy metal-associated protein (AcHMA1) from the halophyte, Atriplex canescens (Pursh) Nutt., confers tolerance to iron and other abiotic stresses when expressed in Saccharomyces cerevisiae.
Auteurs : Xin-Hua Sun [République populaire de Chine] ; Gang Yu [République populaire de Chine] ; Jing-Tao Li [République populaire de Chine] ; Pan Jia [République populaire de Chine] ; Ji-Chao Zhang [République populaire de Chine] ; Cheng-Guo Jia [République populaire de Chine] ; Yan-Hua Zhang [République populaire de Chine] ; Hong-Yu Pan [République populaire de Chine]Source :
- International journal of molecular sciences [ 1422-0067 ] ; 2014.
Descripteurs français
- KwdFr :
- MESH :
- effets des médicaments et des substances chimiques : Saccharomyces cerevisiae.
- génétique : Protéines végétales, Saccharomyces cerevisiae.
- métabolisme : Plantes tolérantes au sel, Protéines végétales, Saccharomyces cerevisiae.
- pharmacologie : Fer.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Plant Proteins.
- chemical , metabolism : Plant Proteins.
- chemical , pharmacology : Iron.
- drug effects : Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae, Salt-Tolerant Plants.
Abstract
Many heavy metals are essential for metabolic processes, but are toxic at elevated levels. Metal tolerance proteins provide resistance to this toxicity. In this study, we identified and characterized a heavy metal-associated protein, AcHMA1, from the halophyte, Atriplex canescens. Sequence analysis has revealed that AcHMA1 contains two heavy metal binding domains. Treatments with metals (Fe, Cu, Ni, Cd or Pb), PEG6000 and NaHCO3 highly induced AcHMA1 expression in A. canescens, whereas NaCl and low temperature decreased its expression. The role of AcHMA1 in metal stress tolerance was examined using a yeast expression system. Expression of the AcHMA1 gene significantly increased the ability of yeast cells to adapt to and recover from exposure to excess iron. AcHMA1 expression also provided salt, alkaline, osmotic and oxidant stress tolerance in yeast cells. Finally, subcellular localization of an AcHMA1/GFP fusion protein expressed in tobacco cells showed that AcHMA1 was localized in the plasma membrane. Thus, our results suggest that AcHMA1 encodes a membrane-localized metal tolerance protein that mediates the detoxification of iron in eukaryotes. Furthermore, AcHMA1 also participates in the response to abiotic stress.
DOI: 10.3390/ijms150814891
PubMed: 25153638
PubMed Central: PMC4159888
Affiliations:
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xml:lang="en">A heavy metal-associated protein (AcHMA1) from the halophyte, Atriplex canescens (Pursh) Nutt., confers tolerance to iron and other abiotic stresses when expressed in Saccharomyces cerevisiae.</title><author><name sortKey="Sun, Xin Hua" sort="Sun, Xin Hua" uniqKey="Sun X" first="Xin-Hua" last="Sun">Xin-Hua Sun</name><affiliation wicri:level="4"><nlm:affiliation>College of Plant Science, Jilin University, Changchun130062, Jilin, China. xinhua_sun@126.com.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>College of Plant Science, Jilin University, Changchun130062, Jilin</wicri:regionArea><orgName type="university">Université de Jilin</orgName><placeName><settlement type="city">Changchun</settlement><region type="province">Jilin</region></placeName></affiliation></author><author><name sortKey="Yu, Gang" sort="Yu, Gang" uniqKey="Yu G" first="Gang" last="Yu">Gang Yu</name><affiliation wicri:level="4"><nlm:affiliation>College of Plant Science, Jilin University, Changchun130062, Jilin, China. chrisyu_gang@126.com.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>College of Plant Science, Jilin University, Changchun130062, Jilin</wicri:regionArea><orgName type="university">Université de Jilin</orgName><placeName><settlement type="city">Changchun</settlement><region type="province">Jilin</region></placeName></affiliation></author><author><name sortKey="Li, Jing Tao" sort="Li, Jing Tao" uniqKey="Li J" first="Jing-Tao" last="Li">Jing-Tao Li</name><affiliation wicri:level="4"><nlm:affiliation>College of Plant Science, Jilin University, Changchun130062, Jilin, China. lijingtao789@126.com.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>College of Plant Science, Jilin University, Changchun130062, Jilin</wicri:regionArea><orgName type="university">Université de Jilin</orgName><placeName><settlement 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zhang_ji_chao@126.com.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>College of Plant Science, Jilin University, Changchun130062, Jilin</wicri:regionArea><orgName type="university">Université de Jilin</orgName><placeName><settlement type="city">Changchun</settlement><region type="province">Jilin</region></placeName></affiliation></author><author><name sortKey="Jia, Cheng Guo" sort="Jia, Cheng Guo" uniqKey="Jia C" first="Cheng-Guo" last="Jia">Cheng-Guo Jia</name><affiliation wicri:level="4"><nlm:affiliation>College of Plant Science, Jilin University, Changchun130062, Jilin, China. jiacg@jlu.edu.cn.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>College of Plant Science, Jilin University, Changchun130062, Jilin</wicri:regionArea><orgName type="university">Université de Jilin</orgName><placeName><settlement type="city">Changchun</settlement><region type="province">Jilin</region></placeName></affiliation></author><author><name sortKey="Zhang, Yan Hua" sort="Zhang, Yan Hua" uniqKey="Zhang Y" first="Yan-Hua" last="Zhang">Yan-Hua Zhang</name><affiliation wicri:level="4"><nlm:affiliation>College of Plant Science, Jilin University, Changchun130062, Jilin, China. yh_zhang@jlu.edu.cn.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>College of Plant Science, Jilin University, Changchun130062, Jilin</wicri:regionArea><orgName type="university">Université de Jilin</orgName><placeName><settlement type="city">Changchun</settlement><region type="province">Jilin</region></placeName></affiliation></author><author><name sortKey="Pan, Hong Yu" sort="Pan, Hong Yu" uniqKey="Pan H" first="Hong-Yu" last="Pan">Hong-Yu Pan</name><affiliation wicri:level="4"><nlm:affiliation>College of Plant Science, Jilin University, Changchun130062, Jilin, China. panhongyu@jlu.edu.cn.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>College of Plant Science, Jilin University, Changchun130062, Jilin</wicri:regionArea><orgName type="university">Université de Jilin</orgName><placeName><settlement type="city">Changchun</settlement><region type="province">Jilin</region></placeName></affiliation></author></analytic><series><title level="j">International journal of molecular sciences</title><idno type="eISSN">1422-0067</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Iron (pharmacology)</term><term>Plant Proteins (genetics)</term><term>Plant Proteins (metabolism)</term><term>Saccharomyces cerevisiae (drug effects)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Salt-Tolerant Plants (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Fer (pharmacologie)</term><term>Plantes tolérantes au sel (métabolisme)</term><term>Protéines végétales (génétique)</term><term>Protéines végétales (métabolisme)</term><term>Saccharomyces cerevisiae (effets des médicaments et des substances chimiques)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Saccharomyces cerevisiae (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Plant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Plant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Iron</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines végétales</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term><term>Salt-Tolerant Plants</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Plantes tolérantes au sel</term><term>Protéines végétales</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Fer</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Many heavy metals are essential for metabolic processes, but are toxic at elevated levels. Metal tolerance proteins provide resistance to this toxicity. In this study, we identified and characterized a heavy metal-associated protein, AcHMA1, from the halophyte, Atriplex canescens. Sequence analysis has revealed that AcHMA1 contains two heavy metal binding domains. Treatments with metals (Fe, Cu, Ni, Cd or Pb), PEG6000 and NaHCO3 highly induced AcHMA1 expression in A. canescens, whereas NaCl and low temperature decreased its expression. The role of AcHMA1 in metal stress tolerance was examined using a yeast expression system. Expression of the AcHMA1 gene significantly increased the ability of yeast cells to adapt to and recover from exposure to excess iron. AcHMA1 expression also provided salt, alkaline, osmotic and oxidant stress tolerance in yeast cells. Finally, subcellular localization of an AcHMA1/GFP fusion protein expressed in tobacco cells showed that AcHMA1 was localized in the plasma membrane. Thus, our results suggest that AcHMA1 encodes a membrane-localized metal tolerance protein that mediates the detoxification of iron in eukaryotes. Furthermore, AcHMA1 also participates in the response to abiotic stress. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25153638</PMID><DateCompleted><Year>2015</Year><Month>06</Month><Day>05</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1422-0067</ISSN><JournalIssue CitedMedium="Internet"><Volume>15</Volume><Issue>8</Issue><PubDate><Year>2014</Year><Month>Aug</Month><Day>22</Day></PubDate></JournalIssue><Title>International journal of molecular sciences</Title><ISOAbbreviation>Int J Mol Sci</ISOAbbreviation></Journal><ArticleTitle>A heavy metal-associated protein (AcHMA1) from the halophyte, Atriplex canescens (Pursh) Nutt., confers tolerance to iron and other abiotic stresses when expressed in Saccharomyces cerevisiae.</ArticleTitle><Pagination><MedlinePgn>14891-906</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.3390/ijms150814891</ELocationID><Abstract><AbstractText>Many heavy metals are essential for metabolic processes, but are toxic at elevated levels. Metal tolerance proteins provide resistance to this toxicity. In this study, we identified and characterized a heavy metal-associated protein, AcHMA1, from the halophyte, Atriplex canescens. Sequence analysis has revealed that AcHMA1 contains two heavy metal binding domains. Treatments with metals (Fe, Cu, Ni, Cd or Pb), PEG6000 and NaHCO3 highly induced AcHMA1 expression in A. canescens, whereas NaCl and low temperature decreased its expression. The role of AcHMA1 in metal stress tolerance was examined using a yeast expression system. Expression of the AcHMA1 gene significantly increased the ability of yeast cells to adapt to and recover from exposure to excess iron. AcHMA1 expression also provided salt, alkaline, osmotic and oxidant stress tolerance in yeast cells. Finally, subcellular localization of an AcHMA1/GFP fusion protein expressed in tobacco cells showed that AcHMA1 was localized in the plasma membrane. Thus, our results suggest that AcHMA1 encodes a membrane-localized metal tolerance protein that mediates the detoxification of iron in eukaryotes. Furthermore, AcHMA1 also participates in the response to abiotic stress. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sun</LastName><ForeName>Xin-Hua</ForeName><Initials>XH</Initials><AffiliationInfo><Affiliation>College of Plant Science, Jilin University, Changchun130062, Jilin, China. xinhua_sun@126.com.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yu</LastName><ForeName>Gang</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>College of Plant Science, Jilin University, Changchun130062, Jilin, China. chrisyu_gang@126.com.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Jing-Tao</ForeName><Initials>JT</Initials><AffiliationInfo><Affiliation>College of Plant Science, Jilin University, Changchun130062, Jilin, China. lijingtao789@126.com.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jia</LastName><ForeName>Pan</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>College of Plant Science, Jilin University, Changchun130062, Jilin, China. jiapanpan1994@126.com.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Ji-Chao</ForeName><Initials>JC</Initials><AffiliationInfo><Affiliation>College of Plant Science, Jilin University, Changchun130062, Jilin, China. zhang_ji_chao@126.com.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jia</LastName><ForeName>Cheng-Guo</ForeName><Initials>CG</Initials><AffiliationInfo><Affiliation>College of Plant Science, Jilin University, Changchun130062, Jilin, China. jiacg@jlu.edu.cn.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Yan-Hua</ForeName><Initials>YH</Initials><AffiliationInfo><Affiliation>College of Plant Science, Jilin University, Changchun130062, Jilin, China. yh_zhang@jlu.edu.cn.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pan</LastName><ForeName>Hong-Yu</ForeName><Initials>HY</Initials><AffiliationInfo><Affiliation>College of Plant Science, Jilin University, Changchun130062, Jilin, China. panhongyu@jlu.edu.cn.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>08</Month><Day>22</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Int J Mol Sci</MedlineTA><NlmUniqueID>101092791</NlmUniqueID><ISSNLinking>1422-0067</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>E1UOL152H7</RegistryNumber><NameOfSubstance UI="D007501">Iron</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D055051" MajorTopicYN="N">Salt-Tolerant Plants</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>07</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2014</Year><Month>08</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>08</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>8</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>8</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>6</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId 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Chine</li></country><region><li>Jilin</li></region><settlement><li>Changchun</li></settlement><orgName><li>Université de Jilin</li></orgName></list><tree><country name="République populaire de Chine"><region name="Jilin"><name sortKey="Sun, Xin Hua" sort="Sun, Xin Hua" uniqKey="Sun X" first="Xin-Hua" last="Sun">Xin-Hua Sun</name></region><name sortKey="Jia, Cheng Guo" sort="Jia, Cheng Guo" uniqKey="Jia C" first="Cheng-Guo" last="Jia">Cheng-Guo Jia</name><name sortKey="Jia, Pan" sort="Jia, Pan" uniqKey="Jia P" first="Pan" last="Jia">Pan Jia</name><name sortKey="Li, Jing Tao" sort="Li, Jing Tao" uniqKey="Li J" first="Jing-Tao" last="Li">Jing-Tao Li</name><name sortKey="Pan, Hong Yu" sort="Pan, Hong Yu" uniqKey="Pan H" first="Hong-Yu" last="Pan">Hong-Yu Pan</name><name sortKey="Yu, Gang" sort="Yu, Gang" uniqKey="Yu G" first="Gang" last="Yu">Gang Yu</name><name sortKey="Zhang, Ji Chao" sort="Zhang, Ji Chao" uniqKey="Zhang J" first="Ji-Chao" last="Zhang">Ji-Chao Zhang</name><name 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|texte= A heavy metal-associated protein (AcHMA1) from the halophyte, Atriplex canescens (Pursh) Nutt., confers tolerance to iron and other abiotic stresses when expressed in Saccharomyces cerevisiae.
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