Metallothionein-like peptides involved in sequestration of Zn in the Zn-accumulating ectomycorrhizal fungus Russula atropurpurea.
Identifieur interne : 001876 ( Main/Exploration ); précédent : 001875; suivant : 001877Metallothionein-like peptides involved in sequestration of Zn in the Zn-accumulating ectomycorrhizal fungus Russula atropurpurea.
Auteurs : Tereza Leonhardt [République tchèque] ; Jan Sáck ; Pavel Šimek ; Ji Šantrů Ek ; Pavel KotrbaSource :
- Metallomics : integrated biometal science [ 1756-591X ] ; 2014.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Analyse de séquence de protéine (MeSH), Basidiomycota (métabolisme), Cadmium (métabolisme), Données de séquences moléculaires (MeSH), Espace intracellulaire (métabolisme), Mutation (génétique), Mycorhizes (métabolisme), Métallothionéine (composition chimique), Métallothionéine (isolement et purification), Métallothionéine (métabolisme), Peptides (composition chimique), Peptides (isolement et purification), Peptides (métabolisme), Saccharomyces cerevisiae (métabolisme), Séquence d'acides aminés (MeSH), Zinc (composition chimique), Zinc (métabolisme).
- MESH :
- composition chimique : Métallothionéine, Peptides, Zinc.
- génétique : Mutation.
- isolement et purification : Métallothionéine, Peptides.
- métabolisme : Basidiomycota, Cadmium, Espace intracellulaire, Mycorhizes, Métallothionéine, Peptides, Saccharomyces cerevisiae, Zinc.
- Alignement de séquences, Analyse de séquence de protéine, Données de séquences moléculaires, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Basidiomycota (metabolism), Cadmium (metabolism), Intracellular Space (metabolism), Metallothionein (chemistry), Metallothionein (isolation & purification), Metallothionein (metabolism), Molecular Sequence Data (MeSH), Mutation (genetics), Mycorrhizae (metabolism), Peptides (chemistry), Peptides (isolation & purification), Peptides (metabolism), Saccharomyces cerevisiae (metabolism), Sequence Alignment (MeSH), Sequence Analysis, Protein (MeSH), Zinc (chemistry), Zinc (metabolism).
- MESH :
- chemical , chemistry : Metallothionein, Peptides, Zinc.
- chemical , isolation & purification : Metallothionein, Peptides.
- chemical , metabolism : Cadmium, Metallothionein, Peptides, Zinc.
- genetics : Mutation.
- metabolism : Basidiomycota, Intracellular Space, Mycorrhizae, Saccharomyces cerevisiae.
- Amino Acid Sequence, Molecular Sequence Data, Sequence Alignment, Sequence Analysis, Protein.
Abstract
Homeostatic mechanisms preventing the toxicity of free Zn ions in cells involve, among others, cytosolic Zn-binding ligands, particularly the cysteine-rich metallothioneins (MTs). Here we examined the Zn-binding peptides of Russula atropurpurea, an ectomycorrhizal fungus known for its ability to accumulate high amounts of Zn in its sporocarps. The Zn complexes and their peptide ligands were characterized using chromatography, electrophoresis after fluorescent labeling of cysteine residues, and tandem mass spectrometry. Functional complementation assays in Saccharomyces cerevisiae were used to obtain and characterize cDNA sequences. Zn-speciation analysis showed that nearly 80% of the Zn extracted from the sporocarps was associated with cysteine-containing peptides in a 5 kDa complex. Screening of an R. atropurpurea cDNA library for sequences encoding peptides capable of sequestering divalent heavy metals was conducted in the Cd-hypersensitive ycf1Δ yeast. This allowed identification of two cDNAs, RaZBP1 and RaZBP2, which protected the metal-sensitive yeast mutants against Cd and Zn, but not Co, Mn or Cu, toxicity. The corresponding RaZBP1 and RaZBP2 peptides consisting of 53 amino acid (AA) residues and sharing 77% identity showed only a limited sequence similarity to known MTs, particularly due to the absence of multiple Cys-AA-Cys motifs. Both RaZBPs were detected in a native Zn-complex of R. atropurpurea and the recombinant RaZBP1 was found associated with Zn and Cd in yeasts. Altogether, the results point to an important role of RaZBPs in the handling of a substantial portion of the Zn pool in R. atropurpurea.
DOI: 10.1039/c4mt00141a
PubMed: 24992964
Affiliations:
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peptides involved in sequestration of Zn in the Zn-accumulating ectomycorrhizal fungus Russula atropurpurea.</title><author><name sortKey="Leonhardt, Tereza" sort="Leonhardt, Tereza" uniqKey="Leonhardt T" first="Tereza" last="Leonhardt">Tereza Leonhardt</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Chemical Technology, Prague, Department of Biochemistry and Microbiology, Technická 3, 166 28 Prague, Czech Republic. pavel.kotrba@vscht.cz.</nlm:affiliation><country xml:lang="fr">République tchèque</country><wicri:regionArea>Institute of Chemical Technology, Prague, Department of Biochemistry and Microbiology, Technická 3, 166 28 Prague</wicri:regionArea><wicri:noRegion>166 28 Prague</wicri:noRegion></affiliation></author><author><name sortKey="Sack, Jan" sort="Sack, Jan" uniqKey="Sack J" first="Jan" last="Sáck">Jan Sáck</name></author><author><name sortKey="Simek, Pavel" sort="Simek, Pavel" uniqKey="Simek P" first="Pavel" last="Šimek">Pavel Šimek</name></author><author><name sortKey="Santru Ek, Ji" sort="Santru Ek, Ji" uniqKey="Santru Ek J" first="Ji" last="Šantrů Ek">Ji Šantrů Ek</name></author><author><name sortKey="Kotrba, Pavel" sort="Kotrba, Pavel" uniqKey="Kotrba P" first="Pavel" last="Kotrba">Pavel Kotrba</name></author></analytic><series><title level="j">Metallomics : integrated biometal science</title><idno type="eISSN">1756-591X</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Basidiomycota (metabolism)</term><term>Cadmium (metabolism)</term><term>Intracellular Space (metabolism)</term><term>Metallothionein (chemistry)</term><term>Metallothionein (isolation & purification)</term><term>Metallothionein (metabolism)</term><term>Molecular Sequence Data (MeSH)</term><term>Mutation (genetics)</term><term>Mycorrhizae (metabolism)</term><term>Peptides (chemistry)</term><term>Peptides (isolation & purification)</term><term>Peptides (metabolism)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Sequence Alignment (MeSH)</term><term>Sequence Analysis, Protein (MeSH)</term><term>Zinc (chemistry)</term><term>Zinc (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Analyse de séquence de protéine (MeSH)</term><term>Basidiomycota (métabolisme)</term><term>Cadmium (métabolisme)</term><term>Données de séquences moléculaires (MeSH)</term><term>Espace intracellulaire (métabolisme)</term><term>Mutation (génétique)</term><term>Mycorhizes (métabolisme)</term><term>Métallothionéine (composition chimique)</term><term>Métallothionéine (isolement et purification)</term><term>Métallothionéine (métabolisme)</term><term>Peptides (composition chimique)</term><term>Peptides (isolement et purification)</term><term>Peptides (métabolisme)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Séquence d'acides aminés (MeSH)</term><term>Zinc (composition chimique)</term><term>Zinc (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Metallothionein</term><term>Peptides</term><term>Zinc</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Metallothionein</term><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cadmium</term><term>Metallothionein</term><term>Peptides</term><term>Zinc</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Métallothionéine</term><term>Peptides</term><term>Zinc</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mutation</term></keywords><keywords scheme="MESH" qualifier="génétique" 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moléculaires</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Homeostatic mechanisms preventing the toxicity of free Zn ions in cells involve, among others, cytosolic Zn-binding ligands, particularly the cysteine-rich metallothioneins (MTs). Here we examined the Zn-binding peptides of Russula atropurpurea, an ectomycorrhizal fungus known for its ability to accumulate high amounts of Zn in its sporocarps. The Zn complexes and their peptide ligands were characterized using chromatography, electrophoresis after fluorescent labeling of cysteine residues, and tandem mass spectrometry. Functional complementation assays in Saccharomyces cerevisiae were used to obtain and characterize cDNA sequences. Zn-speciation analysis showed that nearly 80% of the Zn extracted from the sporocarps was associated with cysteine-containing peptides in a 5 kDa complex. Screening of an R. atropurpurea cDNA library for sequences encoding peptides capable of sequestering divalent heavy metals was conducted in the Cd-hypersensitive ycf1Δ yeast. This allowed identification of two cDNAs, RaZBP1 and RaZBP2, which protected the metal-sensitive yeast mutants against Cd and Zn, but not Co, Mn or Cu, toxicity. The corresponding RaZBP1 and RaZBP2 peptides consisting of 53 amino acid (AA) residues and sharing 77% identity showed only a limited sequence similarity to known MTs, particularly due to the absence of multiple Cys-AA-Cys motifs. Both RaZBPs were detected in a native Zn-complex of R. atropurpurea and the recombinant RaZBP1 was found associated with Zn and Cd in yeasts. Altogether, the results point to an important role of RaZBPs in the handling of a substantial portion of the Zn pool in R. atropurpurea. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24992964</PMID><DateCompleted><Year>2015</Year><Month>04</Month><Day>20</Day></DateCompleted><DateRevised><Year>2014</Year><Month>08</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1756-591X</ISSN><JournalIssue CitedMedium="Internet"><Volume>6</Volume><Issue>9</Issue><PubDate><Year>2014</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Metallomics : integrated biometal science</Title><ISOAbbreviation>Metallomics</ISOAbbreviation></Journal><ArticleTitle>Metallothionein-like peptides involved in sequestration of Zn in the Zn-accumulating ectomycorrhizal fungus Russula atropurpurea.</ArticleTitle><Pagination><MedlinePgn>1693-701</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1039/c4mt00141a</ELocationID><Abstract><AbstractText>Homeostatic mechanisms preventing the toxicity of free Zn ions in cells involve, among others, cytosolic Zn-binding ligands, particularly the cysteine-rich metallothioneins (MTs). Here we examined the Zn-binding peptides of Russula atropurpurea, an ectomycorrhizal fungus known for its ability to accumulate high amounts of Zn in its sporocarps. The Zn complexes and their peptide ligands were characterized using chromatography, electrophoresis after fluorescent labeling of cysteine residues, and tandem mass spectrometry. Functional complementation assays in Saccharomyces cerevisiae were used to obtain and characterize cDNA sequences. Zn-speciation analysis showed that nearly 80% of the Zn extracted from the sporocarps was associated with cysteine-containing peptides in a 5 kDa complex. Screening of an R. atropurpurea cDNA library for sequences encoding peptides capable of sequestering divalent heavy metals was conducted in the Cd-hypersensitive ycf1Δ yeast. This allowed identification of two cDNAs, RaZBP1 and RaZBP2, which protected the metal-sensitive yeast mutants against Cd and Zn, but not Co, Mn or Cu, toxicity. The corresponding RaZBP1 and RaZBP2 peptides consisting of 53 amino acid (AA) residues and sharing 77% identity showed only a limited sequence similarity to known MTs, particularly due to the absence of multiple Cys-AA-Cys motifs. Both RaZBPs were detected in a native Zn-complex of R. atropurpurea and the recombinant RaZBP1 was found associated with Zn and Cd in yeasts. Altogether, the results point to an important role of RaZBPs in the handling of a substantial portion of the Zn pool in R. atropurpurea. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Leonhardt</LastName><ForeName>Tereza</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Institute of Chemical Technology, Prague, Department of Biochemistry and Microbiology, Technická 3, 166 28 Prague, Czech Republic. pavel.kotrba@vscht.cz.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sácký</LastName><ForeName>Jan</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Šimek</LastName><ForeName>Pavel</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Šantrůček</LastName><ForeName>Jiří</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Kotrba</LastName><ForeName>Pavel</ForeName><Initials>P</Initials></Author></AuthorList><Language>eng</Language><DataBankList 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PubStatus="pubmed"><Year>2014</Year><Month>7</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>4</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24992964</ArticleId><ArticleId IdType="doi">10.1039/c4mt00141a</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>République tchèque</li></country></list><tree><noCountry><name sortKey="Kotrba, Pavel" sort="Kotrba, Pavel" uniqKey="Kotrba P" first="Pavel" last="Kotrba">Pavel Kotrba</name><name sortKey="Sack, Jan" sort="Sack, Jan" uniqKey="Sack J" first="Jan" last="Sáck">Jan Sáck</name><name sortKey="Santru Ek, Ji" sort="Santru Ek, Ji" uniqKey="Santru Ek J" first="Ji" last="Šantrů Ek">Ji Šantrů Ek</name><name sortKey="Simek, Pavel" sort="Simek, Pavel" uniqKey="Simek P" first="Pavel" last="Šimek">Pavel Šimek</name></noCountry><country name="République tchèque"><noRegion><name sortKey="Leonhardt, Tereza" sort="Leonhardt, Tereza" uniqKey="Leonhardt T" first="Tereza" last="Leonhardt">Tereza Leonhardt</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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