Metal binding to the N-terminal cytoplasmic domain of the PIB ATPase HMA4 is required for metal transport in Arabidopsis.
Identifieur interne : 000117 ( Main/Corpus ); précédent : 000116; suivant : 000118Metal binding to the N-terminal cytoplasmic domain of the PIB ATPase HMA4 is required for metal transport in Arabidopsis.
Auteurs : Clémentine Laurent ; Gilles Lekeux ; Ashwinie A. Ukuwela ; Zhiguang Xiao ; Jean-Benoit Charlier ; Bernard Bosman ; Monique Carnol ; Patrick Motte ; Christian Damblon ; Moreno Galleni ; Marc HanikenneSource :
- Plant molecular biology [ 1573-5028 ] ; 2016.
English descriptors
- KwdEn :
- Adenosine Triphosphatases (genetics), Adenosine Triphosphatases (metabolism), Amino Acid Motifs (MeSH), Arabidopsis (genetics), Arabidopsis (metabolism), Arabidopsis Proteins (genetics), Arabidopsis Proteins (metabolism), Biological Transport (MeSH), Cadmium (metabolism), Cell Membrane (MeSH), Cloning, Molecular (MeSH), Gene Expression Regulation, Plant (physiology), Magnetic Resonance Spectroscopy (MeSH), Metals (metabolism), Models, Molecular (MeSH), Mutation (MeSH), Protein Binding (MeSH), Protein Conformation (MeSH), Protein Transport (MeSH), Zinc (metabolism).
- MESH :
- chemical , genetics : Adenosine Triphosphatases, Arabidopsis Proteins.
- chemical , metabolism : Adenosine Triphosphatases, Arabidopsis Proteins, Cadmium, Metals, Zinc.
- genetics : Arabidopsis.
- metabolism : Arabidopsis.
- physiology : Gene Expression Regulation, Plant.
- Amino Acid Motifs, Biological Transport, Cell Membrane, Cloning, Molecular, Magnetic Resonance Spectroscopy, Models, Molecular, Mutation, Protein Binding, Protein Conformation, Protein Transport.
Abstract
PIB ATPases are metal cation pumps that transport metals across membranes. These proteins possess N- and C-terminal cytoplasmic extensions that contain Cys- and His-rich high affinity metal binding domains, which may be involved in metal sensing, metal ion selectivity and/or in regulation of the pump activity. The PIB ATPase HMA4 (Heavy Metal ATPase 4) plays a central role in metal homeostasis in Arabidopsis thaliana and has a key function in zinc and cadmium hypertolerance and hyperaccumulation in the extremophile plant species Arabidopsis halleri. Here, we examined the function and structure of the N-terminal cytoplasmic metal-binding domain of HMA4. We mutagenized a conserved CCTSE metal-binding motif in the domain and assessed the impact of the mutations on protein function and localization in planta, on metal-binding properties in vitro and on protein structure by Nuclear Magnetic Resonance spectroscopy. The two Cys residues of the motif are essential for the function, but not for localization, of HMA4 in planta, whereas the Glu residue is important but not essential. These residues also determine zinc coordination and affinity. Zinc binding to the N-terminal domain is thus crucial for HMA4 protein function, whereas it is not required to maintain the protein structure. Altogether, combining in vivo and in vitro approaches in our study provides insights towards the molecular understanding of metal transport and specificity of metal P-type ATPases.
DOI: 10.1007/s11103-016-0429-z
PubMed: 26797794
Links to Exploration step
pubmed:26797794Le document en format XML
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Ukuwela</name><affiliation><nlm:affiliation>School of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC, 3010, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Xiao, Zhiguang" sort="Xiao, Zhiguang" uniqKey="Xiao Z" first="Zhiguang" last="Xiao">Zhiguang Xiao</name><affiliation><nlm:affiliation>School of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC, 3010, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Charlier, Jean Benoit" sort="Charlier, Jean Benoit" uniqKey="Charlier J" first="Jean-Benoit" last="Charlier">Jean-Benoit Charlier</name><affiliation><nlm:affiliation>Department of Life Sciences, Center for Protein Engineering (CIP), University of Liège, 4000, Liège, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Bosman, Bernard" sort="Bosman, Bernard" uniqKey="Bosman B" first="Bernard" last="Bosman">Bernard Bosman</name><affiliation><nlm:affiliation>Laboratory of Plant and Microbial Ecology, Department of Biology, Ecology, Evolution, University of Liège, 4000, Liège, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Carnol, Monique" sort="Carnol, Monique" uniqKey="Carnol M" first="Monique" last="Carnol">Monique Carnol</name><affiliation><nlm:affiliation>Laboratory of Plant and Microbial Ecology, Department of Biology, Ecology, Evolution, University of Liège, 4000, Liège, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Motte, Patrick" sort="Motte, Patrick" uniqKey="Motte P" first="Patrick" last="Motte">Patrick Motte</name><affiliation><nlm:affiliation>Department of Life Sciences, Center for Protein Engineering (CIP), University of Liège, 4000, Liège, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>PhytoSYSTEMS, University of Liège, 4000, Liège, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Damblon, Christian" sort="Damblon, Christian" uniqKey="Damblon C" first="Christian" last="Damblon">Christian Damblon</name><affiliation><nlm:affiliation>Chimie Biologique Structurale, Department of Chemistry, University of Liège, Liège, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Galleni, Moreno" sort="Galleni, Moreno" uniqKey="Galleni M" first="Moreno" last="Galleni">Moreno Galleni</name><affiliation><nlm:affiliation>Department of Life Sciences, Center for Protein Engineering (CIP), University of Liège, 4000, Liège, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Hanikenne, Marc" sort="Hanikenne, Marc" uniqKey="Hanikenne M" first="Marc" last="Hanikenne">Marc Hanikenne</name><affiliation><nlm:affiliation>Department of Life Sciences, Center for Protein Engineering (CIP), University of Liège, 4000, Liège, Belgium. marc.hanikenne@ulg.ac.be.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>PhytoSYSTEMS, University of Liège, 4000, Liège, Belgium. marc.hanikenne@ulg.ac.be.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2016">2016</date><idno type="RBID">pubmed:26797794</idno><idno type="pmid">26797794</idno><idno type="doi">10.1007/s11103-016-0429-z</idno><idno type="wicri:Area/Main/Corpus">000117</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000117</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Metal binding to the N-terminal cytoplasmic domain of the PIB ATPase HMA4 is required for metal transport in Arabidopsis.</title><author><name sortKey="Laurent, Clementine" sort="Laurent, Clementine" uniqKey="Laurent C" first="Clémentine" last="Laurent">Clémentine Laurent</name><affiliation><nlm:affiliation>Department of Life Sciences, Center for Protein Engineering (CIP), University of Liège, 4000, Liège, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Lekeux, Gilles" sort="Lekeux, Gilles" uniqKey="Lekeux G" first="Gilles" last="Lekeux">Gilles Lekeux</name><affiliation><nlm:affiliation>Department of Life Sciences, Center for Protein Engineering (CIP), University of Liège, 4000, Liège, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Ukuwela, Ashwinie A" sort="Ukuwela, Ashwinie A" uniqKey="Ukuwela A" first="Ashwinie A" last="Ukuwela">Ashwinie A. Ukuwela</name><affiliation><nlm:affiliation>School of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC, 3010, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Xiao, Zhiguang" sort="Xiao, Zhiguang" uniqKey="Xiao Z" first="Zhiguang" last="Xiao">Zhiguang Xiao</name><affiliation><nlm:affiliation>School of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC, 3010, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Charlier, Jean Benoit" sort="Charlier, Jean Benoit" uniqKey="Charlier J" first="Jean-Benoit" last="Charlier">Jean-Benoit Charlier</name><affiliation><nlm:affiliation>Department of Life Sciences, Center for Protein Engineering (CIP), University of Liège, 4000, Liège, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Bosman, Bernard" sort="Bosman, Bernard" uniqKey="Bosman B" first="Bernard" last="Bosman">Bernard Bosman</name><affiliation><nlm:affiliation>Laboratory of Plant and Microbial Ecology, Department of Biology, Ecology, Evolution, University of Liège, 4000, Liège, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Carnol, Monique" sort="Carnol, Monique" uniqKey="Carnol M" first="Monique" last="Carnol">Monique Carnol</name><affiliation><nlm:affiliation>Laboratory of Plant and Microbial Ecology, Department of Biology, Ecology, Evolution, University of Liège, 4000, Liège, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Motte, Patrick" sort="Motte, Patrick" uniqKey="Motte P" first="Patrick" last="Motte">Patrick Motte</name><affiliation><nlm:affiliation>Department of Life Sciences, Center for Protein Engineering (CIP), University of Liège, 4000, Liège, Belgium.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>PhytoSYSTEMS, University of Liège, 4000, Liège, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Damblon, Christian" sort="Damblon, Christian" uniqKey="Damblon C" first="Christian" last="Damblon">Christian Damblon</name><affiliation><nlm:affiliation>Chimie Biologique Structurale, Department of Chemistry, University of Liège, Liège, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Galleni, Moreno" sort="Galleni, Moreno" uniqKey="Galleni M" first="Moreno" last="Galleni">Moreno Galleni</name><affiliation><nlm:affiliation>Department of Life Sciences, Center for Protein Engineering (CIP), University of Liège, 4000, Liège, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Hanikenne, Marc" sort="Hanikenne, Marc" uniqKey="Hanikenne M" first="Marc" last="Hanikenne">Marc Hanikenne</name><affiliation><nlm:affiliation>Department of Life Sciences, Center for Protein Engineering (CIP), University of Liège, 4000, Liège, Belgium. marc.hanikenne@ulg.ac.be.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>PhytoSYSTEMS, University of Liège, 4000, Liège, Belgium. marc.hanikenne@ulg.ac.be.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Plant molecular biology</title><idno type="eISSN">1573-5028</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adenosine Triphosphatases (genetics)</term><term>Adenosine Triphosphatases (metabolism)</term><term>Amino Acid Motifs (MeSH)</term><term>Arabidopsis (genetics)</term><term>Arabidopsis (metabolism)</term><term>Arabidopsis Proteins (genetics)</term><term>Arabidopsis Proteins (metabolism)</term><term>Biological Transport (MeSH)</term><term>Cadmium (metabolism)</term><term>Cell Membrane (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>Gene Expression Regulation, Plant (physiology)</term><term>Magnetic Resonance Spectroscopy (MeSH)</term><term>Metals (metabolism)</term><term>Models, Molecular (MeSH)</term><term>Mutation (MeSH)</term><term>Protein Binding (MeSH)</term><term>Protein Conformation (MeSH)</term><term>Protein Transport (MeSH)</term><term>Zinc (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Adenosine Triphosphatases</term><term>Arabidopsis Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adenosine Triphosphatases</term><term>Arabidopsis Proteins</term><term>Cadmium</term><term>Metals</term><term>Zinc</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Gene Expression Regulation, Plant</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term><term>Biological Transport</term><term>Cell Membrane</term><term>Cloning, Molecular</term><term>Magnetic Resonance Spectroscopy</term><term>Models, Molecular</term><term>Mutation</term><term>Protein Binding</term><term>Protein Conformation</term><term>Protein Transport</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">PIB ATPases are metal cation pumps that transport metals across membranes. These proteins possess N- and C-terminal cytoplasmic extensions that contain Cys- and His-rich high affinity metal binding domains, which may be involved in metal sensing, metal ion selectivity and/or in regulation of the pump activity. The PIB ATPase HMA4 (Heavy Metal ATPase 4) plays a central role in metal homeostasis in Arabidopsis thaliana and has a key function in zinc and cadmium hypertolerance and hyperaccumulation in the extremophile plant species Arabidopsis halleri. Here, we examined the function and structure of the N-terminal cytoplasmic metal-binding domain of HMA4. We mutagenized a conserved CCTSE metal-binding motif in the domain and assessed the impact of the mutations on protein function and localization in planta, on metal-binding properties in vitro and on protein structure by Nuclear Magnetic Resonance spectroscopy. The two Cys residues of the motif are essential for the function, but not for localization, of HMA4 in planta, whereas the Glu residue is important but not essential. These residues also determine zinc coordination and affinity. Zinc binding to the N-terminal domain is thus crucial for HMA4 protein function, whereas it is not required to maintain the protein structure. Altogether, combining in vivo and in vitro approaches in our study provides insights towards the molecular understanding of metal transport and specificity of metal P-type ATPases. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26797794</PMID><DateCompleted><Year>2016</Year><Month>07</Month><Day>06</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1573-5028</ISSN><JournalIssue CitedMedium="Internet"><Volume>90</Volume><Issue>4-5</Issue><PubDate><Year>2016</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Plant molecular biology</Title><ISOAbbreviation>Plant Mol Biol</ISOAbbreviation></Journal><ArticleTitle>Metal binding to the N-terminal cytoplasmic domain of the PIB ATPase HMA4 is required for metal transport in Arabidopsis.</ArticleTitle><Pagination><MedlinePgn>453-66</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s11103-016-0429-z</ELocationID><Abstract><AbstractText>PIB ATPases are metal cation pumps that transport metals across membranes. These proteins possess N- and C-terminal cytoplasmic extensions that contain Cys- and His-rich high affinity metal binding domains, which may be involved in metal sensing, metal ion selectivity and/or in regulation of the pump activity. The PIB ATPase HMA4 (Heavy Metal ATPase 4) plays a central role in metal homeostasis in Arabidopsis thaliana and has a key function in zinc and cadmium hypertolerance and hyperaccumulation in the extremophile plant species Arabidopsis halleri. Here, we examined the function and structure of the N-terminal cytoplasmic metal-binding domain of HMA4. We mutagenized a conserved CCTSE metal-binding motif in the domain and assessed the impact of the mutations on protein function and localization in planta, on metal-binding properties in vitro and on protein structure by Nuclear Magnetic Resonance spectroscopy. The two Cys residues of the motif are essential for the function, but not for localization, of HMA4 in planta, whereas the Glu residue is important but not essential. These residues also determine zinc coordination and affinity. Zinc binding to the N-terminal domain is thus crucial for HMA4 protein function, whereas it is not required to maintain the protein structure. Altogether, combining in vivo and in vitro approaches in our study provides insights towards the molecular understanding of metal transport and specificity of metal P-type ATPases. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Laurent</LastName><ForeName>Clémentine</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Department of Life Sciences, Center for Protein Engineering (CIP), University of Liège, 4000, Liège, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lekeux</LastName><ForeName>Gilles</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Department of Life Sciences, Center for Protein Engineering (CIP), University of Liège, 4000, Liège, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ukuwela</LastName><ForeName>Ashwinie A</ForeName><Initials>AA</Initials><AffiliationInfo><Affiliation>School of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC, 3010, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Xiao</LastName><ForeName>Zhiguang</ForeName><Initials>Z</Initials><AffiliationInfo><Affiliation>School of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC, 3010, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Charlier</LastName><ForeName>Jean-Benoit</ForeName><Initials>JB</Initials><AffiliationInfo><Affiliation>Department of Life Sciences, Center for Protein Engineering (CIP), University of Liège, 4000, Liège, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bosman</LastName><ForeName>Bernard</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Laboratory of Plant and Microbial Ecology, Department of Biology, Ecology, Evolution, University of Liège, 4000, Liège, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Carnol</LastName><ForeName>Monique</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Laboratory of Plant and Microbial Ecology, Department of Biology, Ecology, Evolution, University of Liège, 4000, Liège, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Motte</LastName><ForeName>Patrick</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Department of Life Sciences, Center for Protein Engineering (CIP), University of Liège, 4000, Liège, Belgium.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>PhytoSYSTEMS, University of Liège, 4000, Liège, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Damblon</LastName><ForeName>Christian</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Chimie Biologique Structurale, Department of Chemistry, University of Liège, Liège, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Galleni</LastName><ForeName>Moreno</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Life Sciences, Center for Protein Engineering (CIP), University of Liège, 4000, Liège, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hanikenne</LastName><ForeName>Marc</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Life Sciences, Center for Protein Engineering (CIP), University of Liège, 4000, Liège, Belgium. marc.hanikenne@ulg.ac.be.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>PhytoSYSTEMS, University of Liège, 4000, Liège, Belgium. marc.hanikenne@ulg.ac.be.</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>2016</Year><Month>01</Month><Day>21</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Plant Mol Biol</MedlineTA><NlmUniqueID>9106343</NlmUniqueID><ISSNLinking>0167-4412</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029681">Arabidopsis Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008670">Metals</NameOfSubstance></Chemical><Chemical><RegistryNumber>00BH33GNGH</RegistryNumber><NameOfSubstance UI="D002104">Cadmium</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.1.-</RegistryNumber><NameOfSubstance UI="D000251">Adenosine Triphosphatases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.1.3</RegistryNumber><NameOfSubstance UI="C477864">HMA4 protein, Arabidopsis</NameOfSubstance></Chemical><Chemical><RegistryNumber>J41CSQ7QDS</RegistryNumber><NameOfSubstance 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UI="D001692" MajorTopicYN="N">Biological Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002104" MajorTopicYN="N">Cadmium</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002462" MajorTopicYN="N">Cell Membrane</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018506" MajorTopicYN="N">Gene Expression Regulation, Plant</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009682" MajorTopicYN="N">Magnetic Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008670" MajorTopicYN="N">Metals</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D021381" MajorTopicYN="N">Protein Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015032" MajorTopicYN="N">Zinc</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Arabidopsis</Keyword><Keyword MajorTopicYN="N">Metal P-type ATPase</Keyword><Keyword MajorTopicYN="N">Metal binding domain</Keyword><Keyword MajorTopicYN="N">Structure–function analysis</Keyword><Keyword MajorTopicYN="N">Zinc 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