Functional analysis of two genes coding for distinct cation diffusion facilitators of the ectomycorrhizal Zn-accumulating fungus Russula atropurpurea.
Identifieur interne : 001147 ( Main/Exploration ); précédent : 001146; suivant : 001148Functional analysis of two genes coding for distinct cation diffusion facilitators of the ectomycorrhizal Zn-accumulating fungus Russula atropurpurea.
Auteurs : Jan Sáck [République tchèque] ; Tereza Leonhardt [République tchèque] ; Pavel Kotrba [République tchèque]Source :
- Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine [ 1572-8773 ] ; 2016.
Descripteurs français
- KwdFr :
- Activation de la transcription (MeSH), Adaptation physiologique (MeSH), Antifongiques (pharmacologie), Cobalt (pharmacologie), Gènes fongiques (MeSH), Mycorhizes (génétique), Mycorhizes (métabolisme), Protéines de transport membranaire (composition chimique), Protéines de transport membranaire (génétique), Protéines de transport membranaire (métabolisme), Protéines fongiques (composition chimique), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Régulation de l'expression des gènes fongiques (MeSH), Saccharomyces cerevisiae (croissance et développement), Saccharomyces cerevisiae (effets des médicaments et des substances chimiques), Séquence d'acides aminés (MeSH), Tests de sensibilité microbienne (MeSH), Viabilité microbienne (MeSH), Zinc (métabolisme), Zinc (pharmacologie).
- MESH :
- composition chimique : Protéines de transport membranaire, Protéines fongiques.
- croissance et développement : Saccharomyces cerevisiae.
- effets des médicaments et des substances chimiques : Saccharomyces cerevisiae.
- génétique : Mycorhizes, Protéines de transport membranaire, Protéines fongiques.
- métabolisme : Mycorhizes, Protéines de transport membranaire, Protéines fongiques, Zinc.
- pharmacologie : Antifongiques, Cobalt, Zinc.
- Activation de la transcription, Adaptation physiologique, Gènes fongiques, Régulation de l'expression des gènes fongiques, Séquence d'acides aminés, Tests de sensibilité microbienne, Viabilité microbienne.
English descriptors
- KwdEn :
- Adaptation, Physiological (MeSH), Amino Acid Sequence (MeSH), Antifungal Agents (pharmacology), Cobalt (pharmacology), Fungal Proteins (chemistry), Fungal Proteins (genetics), Fungal Proteins (metabolism), Gene Expression Regulation, Fungal (MeSH), Genes, Fungal (MeSH), Membrane Transport Proteins (chemistry), Membrane Transport Proteins (genetics), Membrane Transport Proteins (metabolism), Microbial Sensitivity Tests (MeSH), Microbial Viability (MeSH), Mycorrhizae (genetics), Mycorrhizae (metabolism), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (growth & development), Transcriptional Activation (MeSH), Zinc (metabolism), Zinc (pharmacology).
- MESH :
- chemical , chemistry : Fungal Proteins, Membrane Transport Proteins.
- chemical , genetics : Fungal Proteins, Membrane Transport Proteins.
- chemical , metabolism : Fungal Proteins, Membrane Transport Proteins, Zinc.
- chemical , pharmacology : Antifungal Agents, Cobalt, Zinc.
- drug effects : Saccharomyces cerevisiae.
- genetics : Mycorrhizae.
- growth & development : Saccharomyces cerevisiae.
- metabolism : Mycorrhizae.
- Adaptation, Physiological, Amino Acid Sequence, Gene Expression Regulation, Fungal, Genes, Fungal, Microbial Sensitivity Tests, Microbial Viability, Transcriptional Activation.
Abstract
Russula atropurpurea can accumulate remarkably high concentrations of Zn in its sporocarps. We have previously demonstrated that 40 % of the intracellular Zn in this species is sequestered by MT-like RaZBP peptides. To see what other mechanisms for the handling of the accumulated Zn are available to R. atropurpurea, we searched its transcriptome for cDNAs coding for transporters of the cation diffusion facilitator (CDF) family. The transcriptome search enabled us to identify RaCDF1 and RaCDF2, which were further subjected to functional studies in metal sensitive Saccharomyces cerevisiae. The expression of RaCDF1 and its translational fusion with green fluorescent protein (GFP) protected the yeasts against Zn and Co, but not Cd or Mn, toxicity and led to increased Zn accumulation in the cells. The GFP fluorescence, observed in the RaCDF1::GFP-expressing yeasts on tonoplasts, indicated that the RaCDF1-mediated Zn and Co tolerance was a result of vacuolar sequestration of the metals. The expression of RaCDF2 supported Zn, but not Mn, tolerance in the yeasts and reduced the cellular uptake of Zn, which is congruent with the proposed idea of the Zn-efflux function of RaCDF2, supported by the localization of GFP-derived fluorescence on the plasma membrane of the yeasts expressing functional RaCDF2::GFP. Contrarily, RaCDF2 increased the sensitivity to Co and Cd in the yeasts and significantly promoted Cd uptake, which suggested that it can act as a bidirectional metal transporter. The notion that RaCDF1 and RaCDF2 are genuine CDF transporters in R. atropurputrea was further reinforced by the fact that the RaCDF-associated metal tolerance and uptake phenotypes were lost upon the replacement of histidyl (in RaCDF1) and aspartyl (in RaCDF2), which are highly conserved in the second transmembrane domain and known to be essential for the function of CDF proteins.
DOI: 10.1007/s10534-016-9920-x
PubMed: 26906559
Affiliations:
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(genetics)</term><term>Membrane Transport Proteins (metabolism)</term><term>Microbial Sensitivity Tests (MeSH)</term><term>Microbial Viability (MeSH)</term><term>Mycorrhizae (genetics)</term><term>Mycorrhizae (metabolism)</term><term>Saccharomyces cerevisiae (drug effects)</term><term>Saccharomyces cerevisiae (growth & development)</term><term>Transcriptional Activation (MeSH)</term><term>Zinc (metabolism)</term><term>Zinc (pharmacology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Activation de la transcription (MeSH)</term><term>Adaptation physiologique (MeSH)</term><term>Antifongiques (pharmacologie)</term><term>Cobalt (pharmacologie)</term><term>Gènes fongiques (MeSH)</term><term>Mycorhizes (génétique)</term><term>Mycorhizes (métabolisme)</term><term>Protéines de transport membranaire (composition chimique)</term><term>Protéines de transport membranaire (génétique)</term><term>Protéines de transport membranaire (métabolisme)</term><term>Protéines fongiques (composition chimique)</term><term>Protéines fongiques (génétique)</term><term>Protéines fongiques (métabolisme)</term><term>Régulation de l'expression des gènes fongiques (MeSH)</term><term>Saccharomyces cerevisiae (croissance et développement)</term><term>Saccharomyces cerevisiae (effets des médicaments et des substances chimiques)</term><term>Séquence d'acides aminés (MeSH)</term><term>Tests de sensibilité microbienne (MeSH)</term><term>Viabilité microbienne (MeSH)</term><term>Zinc (métabolisme)</term><term>Zinc (pharmacologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Fungal Proteins</term><term>Membrane Transport Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Fungal Proteins</term><term>Membrane Transport Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fungal Proteins</term><term>Membrane Transport Proteins</term><term>Zinc</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antifungal Agents</term><term>Cobalt</term><term>Zinc</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protéines de transport membranaire</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Saccharomyces cerevisiae</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>Mycorrhizae</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Mycorhizes</term><term>Protéines de transport membranaire</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Mycorrhizae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Mycorhizes</term><term>Protéines de transport membranaire</term><term>Protéines fongiques</term><term>Zinc</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antifongiques</term><term>Cobalt</term><term>Zinc</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Adaptation, Physiological</term><term>Amino Acid Sequence</term><term>Gene Expression Regulation, Fungal</term><term>Genes, Fungal</term><term>Microbial Sensitivity Tests</term><term>Microbial Viability</term><term>Transcriptional Activation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Activation de la transcription</term><term>Adaptation physiologique</term><term>Gènes fongiques</term><term>Régulation de l'expression des gènes fongiques</term><term>Séquence d'acides aminés</term><term>Tests de sensibilité microbienne</term><term>Viabilité microbienne</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Russula atropurpurea can accumulate remarkably high concentrations of Zn in its sporocarps. We have previously demonstrated that 40 % of the intracellular Zn in this species is sequestered by MT-like RaZBP peptides. To see what other mechanisms for the handling of the accumulated Zn are available to R. atropurpurea, we searched its transcriptome for cDNAs coding for transporters of the cation diffusion facilitator (CDF) family. The transcriptome search enabled us to identify RaCDF1 and RaCDF2, which were further subjected to functional studies in metal sensitive Saccharomyces cerevisiae. The expression of RaCDF1 and its translational fusion with green fluorescent protein (GFP) protected the yeasts against Zn and Co, but not Cd or Mn, toxicity and led to increased Zn accumulation in the cells. The GFP fluorescence, observed in the RaCDF1::GFP-expressing yeasts on tonoplasts, indicated that the RaCDF1-mediated Zn and Co tolerance was a result of vacuolar sequestration of the metals. The expression of RaCDF2 supported Zn, but not Mn, tolerance in the yeasts and reduced the cellular uptake of Zn, which is congruent with the proposed idea of the Zn-efflux function of RaCDF2, supported by the localization of GFP-derived fluorescence on the plasma membrane of the yeasts expressing functional RaCDF2::GFP. Contrarily, RaCDF2 increased the sensitivity to Co and Cd in the yeasts and significantly promoted Cd uptake, which suggested that it can act as a bidirectional metal transporter. The notion that RaCDF1 and RaCDF2 are genuine CDF transporters in R. atropurputrea was further reinforced by the fact that the RaCDF-associated metal tolerance and uptake phenotypes were lost upon the replacement of histidyl (in RaCDF1) and aspartyl (in RaCDF2), which are highly conserved in the second transmembrane domain and known to be essential for the function of CDF proteins.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26906559</PMID><DateCompleted><Year>2016</Year><Month>12</Month><Day>13</Day></DateCompleted><DateRevised><Year>2016</Year><Month>12</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1572-8773</ISSN><JournalIssue CitedMedium="Internet"><Volume>29</Volume><Issue>2</Issue><PubDate><Year>2016</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine</Title><ISOAbbreviation>Biometals</ISOAbbreviation></Journal><ArticleTitle>Functional analysis of two genes coding for distinct cation diffusion facilitators of the ectomycorrhizal Zn-accumulating fungus Russula atropurpurea.</ArticleTitle><Pagination><MedlinePgn>349-63</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s10534-016-9920-x</ELocationID><Abstract><AbstractText>Russula atropurpurea can accumulate remarkably high concentrations of Zn in its sporocarps. We have previously demonstrated that 40 % of the intracellular Zn in this species is sequestered by MT-like RaZBP peptides. To see what other mechanisms for the handling of the accumulated Zn are available to R. atropurpurea, we searched its transcriptome for cDNAs coding for transporters of the cation diffusion facilitator (CDF) family. The transcriptome search enabled us to identify RaCDF1 and RaCDF2, which were further subjected to functional studies in metal sensitive Saccharomyces cerevisiae. The expression of RaCDF1 and its translational fusion with green fluorescent protein (GFP) protected the yeasts against Zn and Co, but not Cd or Mn, toxicity and led to increased Zn accumulation in the cells. The GFP fluorescence, observed in the RaCDF1::GFP-expressing yeasts on tonoplasts, indicated that the RaCDF1-mediated Zn and Co tolerance was a result of vacuolar sequestration of the metals. The expression of RaCDF2 supported Zn, but not Mn, tolerance in the yeasts and reduced the cellular uptake of Zn, which is congruent with the proposed idea of the Zn-efflux function of RaCDF2, supported by the localization of GFP-derived fluorescence on the plasma membrane of the yeasts expressing functional RaCDF2::GFP. Contrarily, RaCDF2 increased the sensitivity to Co and Cd in the yeasts and significantly promoted Cd uptake, which suggested that it can act as a bidirectional metal transporter. The notion that RaCDF1 and RaCDF2 are genuine CDF transporters in R. atropurputrea was further reinforced by the fact that the RaCDF-associated metal tolerance and uptake phenotypes were lost upon the replacement of histidyl (in RaCDF1) and aspartyl (in RaCDF2), which are highly conserved in the second transmembrane domain and known to be essential for the function of CDF proteins.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sácký</LastName><ForeName>Jan</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Technická 3, 166 28, Prague, Czech Republic.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Leonhardt</LastName><ForeName>Tereza</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Technická 3, 166 28, Prague, Czech Republic.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kotrba</LastName><ForeName>Pavel</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Technická 3, 166 28, Prague, Czech Republic. pavel.kotrba@vscht.cz.</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>02</Month><Day>23</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biometals</MedlineTA><NlmUniqueID>9208478</NlmUniqueID><ISSNLinking>0966-0844</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000935">Antifungal Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D026901">Membrane Transport Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>3G0H8C9362</RegistryNumber><NameOfSubstance UI="D003035">Cobalt</NameOfSubstance></Chemical><Chemical><RegistryNumber>J41CSQ7QDS</RegistryNumber><NameOfSubstance UI="D015032">Zinc</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000222" MajorTopicYN="N">Adaptation, Physiological</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000935" MajorTopicYN="N">Antifungal Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003035" MajorTopicYN="N">Cobalt</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="N">Gene Expression Regulation, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005800" MajorTopicYN="N">Genes, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D026901" MajorTopicYN="N">Membrane Transport Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008826" MajorTopicYN="N">Microbial Sensitivity Tests</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D050296" MajorTopicYN="N">Microbial Viability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D038821" MajorTopicYN="N">Mycorrhizae</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015533" MajorTopicYN="N">Transcriptional Activation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015032" MajorTopicYN="N">Zinc</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Cation diffusion facilitator (CDF) family</Keyword><Keyword MajorTopicYN="N">Ectomycorrhizal fungi</Keyword><Keyword MajorTopicYN="N">Metal tolerance</Keyword><Keyword MajorTopicYN="N">Russula atropurpurea</Keyword><Keyword MajorTopicYN="N">Zinc transport</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year><Month>02</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>02</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>2</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>2</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>12</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26906559</ArticleId><ArticleId IdType="doi">10.1007/s10534-016-9920-x</ArticleId><ArticleId IdType="pii">10.1007/s10534-016-9920-x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>République tchèque</li></country><region><li>Bohême centrale</li></region><settlement><li>Prague</li></settlement></list><tree><country name="République tchèque"><region name="Bohême centrale"><name sortKey="Sack, Jan" sort="Sack, Jan" uniqKey="Sack J" first="Jan" last="Sáck">Jan Sáck</name></region><name sortKey="Kotrba, Pavel" sort="Kotrba, Pavel" uniqKey="Kotrba P" first="Pavel" last="Kotrba">Pavel Kotrba</name><name sortKey="Leonhardt, Tereza" sort="Leonhardt, Tereza" uniqKey="Leonhardt T" first="Tereza" last="Leonhardt">Tereza Leonhardt</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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