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Intracellular sequestration of cadmium and zinc in ectomycorrhizal fungus Amanita muscaria (Agaricales, Amanitaceae) and characterization of its metallothionein gene
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SYSNO ASEP 0559796 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Intracellular sequestration of cadmium and zinc in ectomycorrhizal fungus Amanita muscaria (Agaricales, Amanitaceae) and characterization of its metallothionein gene Author(s) Sácký, J. (CZ)
Chaloupecká, A. (CZ)
Kaňa, A. (CZ)
Šantrůček, J. (CZ)
Borovička, Jan (UJF-V) RID, ORCID, SAI
Leonhardt, T. (CZ)
Kotrba, P. (CZ)Number of authors 7 Article number 103717 Source Title Fungal Genetics and Biology. - : Academic Press - ISSN 1087-1845
Roč. 162, SEP (2022)Number of pages 10 s. Publication form Print - P Language eng - English Country US - United States Keywords Macrofung ; Metal pollution ; Metal accumulation ; Amanita ; Russula ; Metal binding peptides OECD category Genetics and heredity (medical genetics to be 3) Method of publishing Limited access Institutional support UJF-V - RVO:61389005 UT WOS 000830255600001 EID SCOPUS 85148313836 DOI 10.1016/j.fgb.2022.103717 Annotation Amanita muscaria is an ectomycorrhizal mushroom that commonly grows at metal-polluted sites. Sporocarps from the lead smelter-polluted area near Pribram (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 Pribram 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. Workplace Nuclear Physics Institute Contact Markéta Sommerová, sommerova@ujf.cas.cz, Tel.: 266 173 228 Year of Publishing 2023 Electronic address https://doi.org/10.1016/j.fgb.2022.103717
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