CadA of Mesorhizobium metallidurans isolated from a zinc-rich mining soil is a P(IB-2)-type ATPase involved in cadmium and zinc resistance.
Identifieur interne : 000161 ( Main/Corpus ); précédent : 000160; suivant : 000162CadA of Mesorhizobium metallidurans isolated from a zinc-rich mining soil is a P(IB-2)-type ATPase involved in cadmium and zinc resistance.
Auteurs : Geraldine Maynaud ; Brigitte Brunel ; Erika Yashiro ; Max Mergeay ; Jean-Claude Cleyet-Marel ; Antoine Le QuéréSource :
- Research in microbiology [ 1769-7123 ] ; 2014.
English descriptors
- KwdEn :
- Adenosine Triphosphatases (genetics), Adenosine Triphosphatases (metabolism), Amino Acid Sequence (MeSH), Binding Sites (MeSH), Cadmium (toxicity), Drug Resistance, Bacterial (MeSH), Fabaceae (microbiology), Gene Deletion (MeSH), Gene Expression Profiling (MeSH), Genes, Reporter (MeSH), Green Fluorescent Proteins (analysis), Mesorhizobium (enzymology), Mesorhizobium (isolation & purification), Molecular Sequence Data (MeSH), Plant Root Nodulation (MeSH), Protein Binding (MeSH), Sequence Alignment (MeSH), Soil Microbiology (MeSH), Zinc (toxicity).
- MESH :
- chemical , analysis : Green Fluorescent Proteins.
- chemical , genetics : Adenosine Triphosphatases.
- chemical , metabolism : Adenosine Triphosphatases.
- chemical , toxicity : Cadmium, Zinc.
- enzymology : Mesorhizobium.
- isolation & purification : Mesorhizobium.
- microbiology : Fabaceae.
- Amino Acid Sequence, Binding Sites, Drug Resistance, Bacterial, Gene Deletion, Gene Expression Profiling, Genes, Reporter, Molecular Sequence Data, Plant Root Nodulation, Protein Binding, Sequence Alignment, Soil Microbiology.
Abstract
Mesorhizobium metallidurans STM 2683(T) is a nitrogen-fixing bacterium that nodulates Anthyllis vulneraria in mine tailings highly contaminated in zinc, lead and cadmium. To study the mechanisms whereby this bacterium copes with metals, we functionally screened a cosmid genomic library of M. metallidurans for zinc or cadmium tolerance. A cosmid clone harbored a gene encoding P(IB)-type ATPase homologous to CadA that leads to cadmium and zinc resistance in Escherichia coli. The CadA protein structure presents one duplication of the two N-terminal metal binding domains (i.e. a heavy metal-associated domain followed by a histidine-rich domain) which allows specific binding to zinc and cadmium cations. A cadA-deleted strain of M. metallidurans failed to grow at high zinc concentrations (2 mM) and its growth was delayed at lower zinc concentrations. Expression studies using a transcriptional fusion of cadA promoter to gfp showed that cadA is specifically induced in a dose-dependent manner by zinc and cadmium in M. metallidurans in vitro conditions and into A. vulneraria nodules after Zn stress. Metal induction sensitivity was increased in the strain where cadA gene was deleted. This study identified cadA as a first mesorhizobial resistance determinant involved in detoxification of cadmium and zinc and which confers upon M. metallidurans greater capacity for coping with high zinc concentrations. This improves the knowledge of this bacterium for potential use as a symbiotic inoculant of Anthyllis in phytostabilization strategies of metal-rich sites.
DOI: 10.1016/j.resmic.2014.02.001
PubMed: 24607711
Links to Exploration step
pubmed:24607711Le document en format XML
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Electronic address: brunel@supagro.inra.fr.</nlm:affiliation></affiliation></author><author><name sortKey="Yashiro, Erika" sort="Yashiro, Erika" uniqKey="Yashiro E" first="Erika" last="Yashiro">Erika Yashiro</name><affiliation><nlm:affiliation>Montpellier SupAgro, Université Montpellier II, TA A-82/J, 34398 Montpellier Cedex 5, France. Electronic address: erika.yashiro@unil.ch.</nlm:affiliation></affiliation></author><author><name sortKey="Mergeay, Max" sort="Mergeay, Max" uniqKey="Mergeay M" first="Max" last="Mergeay">Max Mergeay</name><affiliation><nlm:affiliation>Molecular and Cellular Biology, Unit Microbiology, Belgian Nuclear Research Center (SCK CEN), Boeretang 200, B-2400 Mol, Belgium. Electronic address: mmergeay@sckcen.be.</nlm:affiliation></affiliation></author><author><name sortKey="Cleyet Marel, Jean Claude" sort="Cleyet Marel, Jean Claude" uniqKey="Cleyet Marel J" first="Jean-Claude" last="Cleyet-Marel">Jean-Claude Cleyet-Marel</name><affiliation><nlm:affiliation>INRA USC1242, Université Montpellier II, TA A-82/J, 34398 Montpellier Cedex 5, France. Electronic address: cleyet@supagro.inra.fr.</nlm:affiliation></affiliation></author><author><name sortKey="Le Quere, Antoine" sort="Le Quere, Antoine" uniqKey="Le Quere A" first="Antoine" last="Le Quéré">Antoine Le Quéré</name><affiliation><nlm:affiliation>IRD, Laboratoire des Symbioses Tropicales et Méditerranéennes UMR113, IRD/INRA/CIRAD/Montpellier SupAgro/Université Montpellier II, TA A-82/J, 34398 Montpellier Cedex 5, France. 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Electronic address: geraldine.maynaud@ird.fr.</nlm:affiliation></affiliation></author><author><name sortKey="Brunel, Brigitte" sort="Brunel, Brigitte" uniqKey="Brunel B" first="Brigitte" last="Brunel">Brigitte Brunel</name><affiliation><nlm:affiliation>Montpellier SupAgro, Université Montpellier II, TA A-82/J, 34398 Montpellier Cedex 5, France. Electronic address: brunel@supagro.inra.fr.</nlm:affiliation></affiliation></author><author><name sortKey="Yashiro, Erika" sort="Yashiro, Erika" uniqKey="Yashiro E" first="Erika" last="Yashiro">Erika Yashiro</name><affiliation><nlm:affiliation>Montpellier SupAgro, Université Montpellier II, TA A-82/J, 34398 Montpellier Cedex 5, France. Electronic address: erika.yashiro@unil.ch.</nlm:affiliation></affiliation></author><author><name sortKey="Mergeay, Max" sort="Mergeay, Max" uniqKey="Mergeay M" first="Max" last="Mergeay">Max Mergeay</name><affiliation><nlm:affiliation>Molecular and Cellular Biology, Unit Microbiology, Belgian Nuclear Research Center (SCK CEN), Boeretang 200, B-2400 Mol, Belgium. Electronic address: mmergeay@sckcen.be.</nlm:affiliation></affiliation></author><author><name sortKey="Cleyet Marel, Jean Claude" sort="Cleyet Marel, Jean Claude" uniqKey="Cleyet Marel J" first="Jean-Claude" last="Cleyet-Marel">Jean-Claude Cleyet-Marel</name><affiliation><nlm:affiliation>INRA USC1242, Université Montpellier II, TA A-82/J, 34398 Montpellier Cedex 5, France. Electronic address: cleyet@supagro.inra.fr.</nlm:affiliation></affiliation></author><author><name sortKey="Le Quere, Antoine" sort="Le Quere, Antoine" uniqKey="Le Quere A" first="Antoine" last="Le Quéré">Antoine Le Quéré</name><affiliation><nlm:affiliation>IRD, Laboratoire des Symbioses Tropicales et Méditerranéennes UMR113, IRD/INRA/CIRAD/Montpellier SupAgro/Université Montpellier II, TA A-82/J, 34398 Montpellier Cedex 5, France. Electronic address: antoine.le-quere@ird.fr.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Research in microbiology</title><idno type="eISSN">1769-7123</idno><imprint><date when="2014" type="published">2014</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 Sequence (MeSH)</term><term>Binding Sites (MeSH)</term><term>Cadmium (toxicity)</term><term>Drug Resistance, Bacterial (MeSH)</term><term>Fabaceae (microbiology)</term><term>Gene Deletion (MeSH)</term><term>Gene Expression Profiling (MeSH)</term><term>Genes, Reporter (MeSH)</term><term>Green Fluorescent Proteins (analysis)</term><term>Mesorhizobium (enzymology)</term><term>Mesorhizobium (isolation & purification)</term><term>Molecular Sequence Data (MeSH)</term><term>Plant Root Nodulation (MeSH)</term><term>Protein Binding (MeSH)</term><term>Sequence Alignment (MeSH)</term><term>Soil Microbiology (MeSH)</term><term>Zinc (toxicity)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Green Fluorescent Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Adenosine Triphosphatases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adenosine Triphosphatases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Cadmium</term><term>Zinc</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Mesorhizobium</term></keywords><keywords scheme="MESH" qualifier="isolation & purification" xml:lang="en"><term>Mesorhizobium</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Fabaceae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Binding Sites</term><term>Drug Resistance, Bacterial</term><term>Gene Deletion</term><term>Gene Expression Profiling</term><term>Genes, Reporter</term><term>Molecular Sequence Data</term><term>Plant Root Nodulation</term><term>Protein Binding</term><term>Sequence Alignment</term><term>Soil Microbiology</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Mesorhizobium metallidurans STM 2683(T) is a nitrogen-fixing bacterium that nodulates Anthyllis vulneraria in mine tailings highly contaminated in zinc, lead and cadmium. To study the mechanisms whereby this bacterium copes with metals, we functionally screened a cosmid genomic library of M. metallidurans for zinc or cadmium tolerance. A cosmid clone harbored a gene encoding P(IB)-type ATPase homologous to CadA that leads to cadmium and zinc resistance in Escherichia coli. The CadA protein structure presents one duplication of the two N-terminal metal binding domains (i.e. a heavy metal-associated domain followed by a histidine-rich domain) which allows specific binding to zinc and cadmium cations. A cadA-deleted strain of M. metallidurans failed to grow at high zinc concentrations (2 mM) and its growth was delayed at lower zinc concentrations. Expression studies using a transcriptional fusion of cadA promoter to gfp showed that cadA is specifically induced in a dose-dependent manner by zinc and cadmium in M. metallidurans in vitro conditions and into A. vulneraria nodules after Zn stress. Metal induction sensitivity was increased in the strain where cadA gene was deleted. This study identified cadA as a first mesorhizobial resistance determinant involved in detoxification of cadmium and zinc and which confers upon M. metallidurans greater capacity for coping with high zinc concentrations. This improves the knowledge of this bacterium for potential use as a symbiotic inoculant of Anthyllis in phytostabilization strategies of metal-rich sites.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24607711</PMID><DateCompleted><Year>2014</Year><Month>12</Month><Day>01</Day></DateCompleted><DateRevised><Year>2014</Year><Month>04</Month><Day>22</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1769-7123</ISSN><JournalIssue CitedMedium="Internet"><Volume>165</Volume><Issue>3</Issue><PubDate><Year>2014</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Research in microbiology</Title><ISOAbbreviation>Res Microbiol</ISOAbbreviation></Journal><ArticleTitle>CadA of Mesorhizobium metallidurans isolated from a zinc-rich mining soil is a P(IB-2)-type ATPase involved in cadmium and zinc resistance.</ArticleTitle><Pagination><MedlinePgn>175-89</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.resmic.2014.02.001</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0923-2508(14)00023-0</ELocationID><Abstract><AbstractText>Mesorhizobium metallidurans STM 2683(T) is a nitrogen-fixing bacterium that nodulates Anthyllis vulneraria in mine tailings highly contaminated in zinc, lead and cadmium. To study the mechanisms whereby this bacterium copes with metals, we functionally screened a cosmid genomic library of M. metallidurans for zinc or cadmium tolerance. A cosmid clone harbored a gene encoding P(IB)-type ATPase homologous to CadA that leads to cadmium and zinc resistance in Escherichia coli. The CadA protein structure presents one duplication of the two N-terminal metal binding domains (i.e. a heavy metal-associated domain followed by a histidine-rich domain) which allows specific binding to zinc and cadmium cations. A cadA-deleted strain of M. metallidurans failed to grow at high zinc concentrations (2 mM) and its growth was delayed at lower zinc concentrations. Expression studies using a transcriptional fusion of cadA promoter to gfp showed that cadA is specifically induced in a dose-dependent manner by zinc and cadmium in M. metallidurans in vitro conditions and into A. vulneraria nodules after Zn stress. Metal induction sensitivity was increased in the strain where cadA gene was deleted. This study identified cadA as a first mesorhizobial resistance determinant involved in detoxification of cadmium and zinc and which confers upon M. metallidurans greater capacity for coping with high zinc concentrations. This improves the knowledge of this bacterium for potential use as a symbiotic inoculant of Anthyllis in phytostabilization strategies of metal-rich sites.</AbstractText><CopyrightInformation>Copyright © 2014 Institut Pasteur. Published by Elsevier Masson SAS. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Maynaud</LastName><ForeName>Geraldine</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>INRA USC1242, Université Montpellier II, TA A-82/J, 34398 Montpellier Cedex 5, France. Electronic address: geraldine.maynaud@ird.fr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Brunel</LastName><ForeName>Brigitte</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Montpellier SupAgro, Université Montpellier II, TA A-82/J, 34398 Montpellier Cedex 5, France. Electronic address: brunel@supagro.inra.fr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yashiro</LastName><ForeName>Erika</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Montpellier SupAgro, Université Montpellier II, TA A-82/J, 34398 Montpellier Cedex 5, France. Electronic address: erika.yashiro@unil.ch.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mergeay</LastName><ForeName>Max</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Molecular and Cellular Biology, Unit Microbiology, Belgian Nuclear Research Center (SCK CEN), Boeretang 200, B-2400 Mol, Belgium. Electronic address: mmergeay@sckcen.be.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cleyet-Marel</LastName><ForeName>Jean-Claude</ForeName><Initials>JC</Initials><AffiliationInfo><Affiliation>INRA USC1242, Université Montpellier II, TA A-82/J, 34398 Montpellier Cedex 5, France. Electronic address: cleyet@supagro.inra.fr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Le Quéré</LastName><ForeName>Antoine</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>IRD, Laboratoire des Symbioses Tropicales et Méditerranéennes UMR113, IRD/INRA/CIRAD/Montpellier SupAgro/Université Montpellier II, TA A-82/J, 34398 Montpellier Cedex 5, France. Electronic address: antoine.le-quere@ird.fr.</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>03</Month><Day>05</Day></ArticleDate></Article><MedlineJournalInfo><Country>France</Country><MedlineTA>Res Microbiol</MedlineTA><NlmUniqueID>8907468</NlmUniqueID><ISSNLinking>0923-2508</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>00BH33GNGH</RegistryNumber><NameOfSubstance UI="D002104">Cadmium</NameOfSubstance></Chemical><Chemical><RegistryNumber>147336-22-9</RegistryNumber><NameOfSubstance UI="D049452">Green Fluorescent Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.1.-</RegistryNumber><NameOfSubstance UI="D000251">Adenosine Triphosphatases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.1.-</RegistryNumber><NameOfSubstance UI="C059771">cadmium translocating ATPase</NameOfSubstance></Chemical><Chemical><RegistryNumber>J41CSQ7QDS</RegistryNumber><NameOfSubstance UI="D015032">Zinc</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000251" MajorTopicYN="N">Adenosine Triphosphatases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002104" MajorTopicYN="N">Cadmium</DescriptorName><QualifierName UI="Q000633" MajorTopicYN="Y">toxicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D024881" MajorTopicYN="Y">Drug Resistance, Bacterial</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007887" MajorTopicYN="N">Fabaceae</DescriptorName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017353" MajorTopicYN="N">Gene Deletion</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020869" MajorTopicYN="N">Gene Expression Profiling</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017930" MajorTopicYN="N">Genes, Reporter</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D049452" MajorTopicYN="N">Green Fluorescent Proteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D059128" MajorTopicYN="N">Mesorhizobium</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055170" MajorTopicYN="N">Plant Root Nodulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012988" MajorTopicYN="Y">Soil Microbiology</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015032" MajorTopicYN="N">Zinc</DescriptorName><QualifierName UI="Q000633" MajorTopicYN="Y">toxicity</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Mesorhizobium</Keyword><Keyword MajorTopicYN="N">Metal efflux transporter</Keyword><Keyword MajorTopicYN="N">Metal tolerance</Keyword><Keyword MajorTopicYN="N">P(IB)-type ATPase</Keyword><Keyword MajorTopicYN="N">cadA transcription</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>05</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>02</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>3</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>3</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>12</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24607711</ArticleId><ArticleId IdType="pii">S0923-2508(14)00023-0</ArticleId><ArticleId IdType="doi">10.1016/j.resmic.2014.02.001</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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