Intracellular sequestration of cadmium and zinc in ectomycorrhizal fungus Amanita muscaria (Agaricales, Amanitaceae) and characterization of its metallothionein gene
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985831%3A_____%2F22%3A00558890" target="_blank" >RIV/67985831:_____/22:00558890 - isvavai.cz</a>
Alternative codes found
RIV/61389005:_____/22:00559796
Result on the web
<a href="https://www.sciencedirect.com/science/article/pii/S1087184522000627" target="_blank" >https://www.sciencedirect.com/science/article/pii/S1087184522000627</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.fgb.2022.103717" target="_blank" >10.1016/j.fgb.2022.103717</a>
Alternative languages
Result language
angličtina
Original language name
Intracellular sequestration of cadmium and zinc in ectomycorrhizal fungus Amanita muscaria (Agaricales, Amanitaceae) and characterization of its metallothionein gene
Original language description
Amanita muscaria is an ectomycorrhizal mushroom that commonly grows at metal-polluted sites. Sporocarps from the lead smelter-polluted area near Příbram (Central Bohemia, Czech Republic) showed elevated concentrations of Cd and Zn. Size exclusion chromatography of the cell extracts of the sporocarps from both polluted and unpolluted sites indicated that substantial part of intracellular Cd and Zn was sequestered in 6-kDa complexes, presumably with metallothionein(s) (MT). When the cultured mycelial isolates were compared, those from Příbram were more Cd-tolerant and accumulated slightly less Cd and Zn than those from the unpolluted site. The analysis of the available A. muscaria sequence data returned a 67-amino acid (AA) MT encoded by the AmMT1 gene. Weak Cd and Zn responsiveness of AmMT1 in the mycelia suggested its metal homeostasis function in A. muscaria, rather than a major role in detoxification. The AmMT1 belongs to a ubiquitous peptide group in the Agaricomycetes consisting of 60–70-AA MTs containing seven cysteinyl domains and a conserved histidyl, features observed also in a newly predicted, atypical 45-AA RaMT1 of the Zn-accumulator Russula bresadolae in which the C-terminal cysteinyl domains VI and VII are missing. Heterologous expression in metal-sensitive yeast mutants indicated that AmMT1 and RaMT1 encode functional peptides that can protect cells against Cd, Zn, and Cu toxicity. The metal protection phenotype observed in yeasts with mutant variants of AmMT1 and RaMT1 further indicated that the conserved histidyl seems to play a structural, not metal binding role, and the cysteinyls of the C-terminal domains VI and VII are important for Cu binding. The data provide an important insight into the metal handling of site-associated ectomycorrhizal species disturbed by excess metals and the properties of MTs common in Agaricomycetes.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
<a href="/en/project/GA19-06759S" target="_blank" >GA19-06759S: Cadmium hyperaccumulation in macrofungi: from isotopes to proteins and bacterial communities</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Fungal Genetics and Biology
ISSN
1087-1845
e-ISSN
1096-0937
Volume of the periodical
162
Issue of the periodical within the volume
September 2022
Country of publishing house
US - UNITED STATES
Number of pages
10
Pages from-to
103717
UT code for WoS article
000830255600001
EID of the result in the Scopus database
2-s2.0-85133246313