Three metallothionein isoforms and sequestration of intracellular silver in the hyperaccumulator Amanita strobiliformis

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F11%3A10082569" target="_blank" >RIV/00216208:11310/11:10082569 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388971:_____/11:00360138 RIV/61389005:_____/11:00360138 RIV/60461373:22330/11:43891712

Výsledek na webu

<a href="http://onlinelibrary.wiley.com/doi/10.1111/j.1469-8137.2010.03634.x/pdf" target="_blank" >http://onlinelibrary.wiley.com/doi/10.1111/j.1469-8137.2010.03634.x/pdf</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1111/j.1469-8137.2010.03634.x" target="_blank" >10.1111/j.1469-8137.2010.03634.x</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Three metallothionein isoforms and sequestration of intracellular silver in the hyperaccumulator Amanita strobiliformis

Popis výsledku v původním jazyce

Metallothioneins (MTs) are cysteine-rich peptides involved in heavy metal tolerance of many eukaryotes. Here, we examined their involvement in intracellular binding of silver (Ag) in the ectomycorrhizal fungus Amanita strobiliformis. The Ag complexes andtheir peptide ligands were characterized using chromatography and mass spectrometry. The full-length coding sequences obtained from a cDNA library were used for complementation assays in yeast mutant strains. Abundance of respective transcripts in A. strobiliformis was measured by quantitative real-time reverse-transcribed polymerase chain reaction (qRT-PCR). Ag-speciation analyses showed that intracellular Ag was in wild-grown fruit bodies and cultured extraradical mycelia of A. strobiliformis sequestered by metallothioneins. The determined sequence of the peptide facilitated isolation of three cDNA clones, AsMT1a, AsMT1b and AsMT1c. These encode isomorphic MTs consisting of 34 amino acid residues and sharing 82% identity.

Název v anglickém jazyce

Three metallothionein isoforms and sequestration of intracellular silver in the hyperaccumulator Amanita strobiliformis

Popis výsledku anglicky

Metallothioneins (MTs) are cysteine-rich peptides involved in heavy metal tolerance of many eukaryotes. Here, we examined their involvement in intracellular binding of silver (Ag) in the ectomycorrhizal fungus Amanita strobiliformis. The Ag complexes andtheir peptide ligands were characterized using chromatography and mass spectrometry. The full-length coding sequences obtained from a cDNA library were used for complementation assays in yeast mutant strains. Abundance of respective transcripts in A. strobiliformis was measured by quantitative real-time reverse-transcribed polymerase chain reaction (qRT-PCR). Ag-speciation analyses showed that intracellular Ag was in wild-grown fruit bodies and cultured extraradical mycelia of A. strobiliformis sequestered by metallothioneins. The determined sequence of the peptide facilitated isolation of three cDNA clones, AsMT1a, AsMT1b and AsMT1c. These encode isomorphic MTs consisting of 34 amino acid residues and sharing 82% identity.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2011

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

New Phytologist

ISSN

0028-646X

e-ISSN

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Svazek periodika

190

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

11

Strana od-do

916-926

Kód UT WoS článku

000290449600013

EID výsledku v databázi Scopus

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