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Statements

Subject Item
n2:RIV%2F60461373%3A22330%2F14%3A43897710%21RIV15-GA0-22330___
rdf:type
n8:Vysledek skos:Concept
rdfs:seeAlso
http://pubs.rsc.org/en/Content/ArticleLanding/2014/MT/C4MT00141A#!divAbstract
dcterms:description
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 ycf1 Delta 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. 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 ycf1 Delta 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.
dcterms:title
Metallothionein-like peptides involved in sequestration of Zn in the Zn-accumulating ectomycorrhizal fungus Russula atropurpurea Metallothionein-like peptides involved in sequestration of Zn in the Zn-accumulating ectomycorrhizal fungus Russula atropurpurea
skos:prefLabel
Metallothionein-like peptides involved in sequestration of Zn in the Zn-accumulating ectomycorrhizal fungus Russula atropurpurea Metallothionein-like peptides involved in sequestration of Zn in the Zn-accumulating ectomycorrhizal fungus Russula atropurpurea
skos:notation
RIV/60461373:22330/14:43897710!RIV15-GA0-22330___
n4:aktivita
n17:P
n4:aktivity
P(GAP504/11/0484)
n4:cisloPeriodika
9
n4:dodaniDat
n19:2015
n4:domaciTvurceVysledku
n6:5077184 n6:1120530 n6:3431134 n6:5894891 n6:2195143
n4:druhVysledku
n14:J
n4:duvernostUdaju
n9:S
n4:entitaPredkladatele
n12:predkladatel
n4:idSjednocenehoVysledku
28570
n4:idVysledku
RIV/60461373:22330/14:43897710
n4:jazykVysledku
n18:eng
n4:klicovaSlova
Zinc binding; Metallothionein; Metal tolerance; Sporocarp; Fungi
n4:klicoveSlovo
n13:Sporocarp n13:Zinc%20binding n13:Metallothionein n13:Metal%20tolerance n13:Fungi
n4:kodStatuVydavatele
GB - Spojené království Velké Británie a Severního Irska
n4:kontrolniKodProRIV
[83AD0EC3F15D]
n4:nazevZdroje
Metallomics
n4:obor
n15:EB
n4:pocetDomacichTvurcuVysledku
5
n4:pocetTvurcuVysledku
5
n4:projekt
n20:GAP504%2F11%2F0484
n4:rokUplatneniVysledku
n19:2014
n4:svazekPeriodika
6
n4:tvurceVysledku
Šantrůček, Jiří Kotrba, Pavel Sácký, Jan Šimek, Pavel Leonhardt, Tereza
n4:wos
000341018500014
s:issn
1756-5901
s:numberOfPages
9
n3:doi
10.1039/c4mt00141a
n16:organizacniJednotka
22330