A Potential Involvement of Metallothionein in the Zinc Tolerance of Trichoderma harzianum: Experimental Findings

IF 1.9 4区生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY The Protein Journal Pub Date : 2024-03-15 DOI:10.1007/s10930-024-10185-1

Negin Ejmalian, Soheila Mirzaei, Asghar Mirzaie-Asl, Mehrdad chaichi

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Abstract

Metallothioneins are a group of cysteine-rich proteins that play an important role in the homeostasis and detoxification of heavy metals. The objective of this research was to explore the significance of metallothionein in Trichoderma harzianum tolerance to zinc. At the inhibitory concentration of 1000 ppm, the fungus adsorbed 16.7 ± 0.4 mg/g of metal. The HPLC and SDS-PAGE electrophoresis data suggested that the fungus production of metallothionein was twice as high in the presence of zinc as in the control group. The examination of the genes; metallothionein expression activator (MEA) and Cu fist revealed that the MEA, with a C₂H₂ zinc finger domain, increased significantly in the presence of zinc. It was observed that in T. harzianum, the enhanced expression of the metallothionein gene was managed by the metallothionein activator under zinc overload conditions. According to our knowledge, this is the first report on the role of metallothionein in the resistance of T. harzianum to zinc.

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金属硫蛋白在哈茨毛霉耐锌性中的潜在参与：实验结果。

金属硫蛋白是一组富含半胱氨酸的蛋白质，在重金属的平衡和解毒过程中发挥着重要作用。本研究的目的是探讨金属硫蛋白在毛霉对锌的耐受性中的重要作用。在抑制浓度为 1000 ppm 时，真菌吸附了 16.7 ± 0.4 mg/g 的金属。HPLC 和 SDS-PAGE 电泳数据表明，在锌存在的情况下，真菌金属硫蛋白的产量是对照组的两倍。对金属硫蛋白表达激活因子（MEA）和铜拳基因的研究表明，具有 C2H2 锌指结构域的 MEA 在锌存在时显著增加。据观察，在T. harzianum中，锌超载条件下金属硫蛋白基因的表达增强是由金属硫蛋白激活剂控制的。据我们所知，这是首次报道金属硫蛋白在哈茨酵母抗锌过程中的作用。

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来源期刊

The Protein Journal 生物-生化与分子生物学

CiteScore

5.20

自引率

0.00%

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审稿时长

12 months

期刊介绍： The Protein Journal (formerly the Journal of Protein Chemistry) publishes original research work on all aspects of proteins and peptides. These include studies concerned with covalent or three-dimensional structure determination (X-ray, NMR, cryoEM, EPR/ESR, optical methods, etc.), computational aspects of protein structure and function, protein folding and misfolding, assembly, genetics, evolution, proteomics, molecular biology, protein engineering, protein nanotechnology, protein purification and analysis and peptide synthesis, as well as the elucidation and interpretation of the molecular bases of biological activities of proteins and peptides. We accept original research papers, reviews, mini-reviews, hypotheses, opinion papers, and letters to the editor.