Abstract
Metallothionein (MT) gene has an important role in the detoxification of toxic metals especially some heavy metals. Based on the published sequences of MT genes from Agaricus bisporus, Garnoderma lucidum, Taiwanofungus camphoratus and Paxillus involutus as a type of the edible or medical mushroom in NCBI database, their molecular structures, physiological functions and evolutionary relationship were analyzed using the bioinformatics methods. Results showed that AbMT, GlMT, TcMT and PiMT genes contained complete open reading frame (ORF) and their theoretical points of the last three encoding proteins were higher than 7.0. AbMT, GlMT, TcMT and PiMT were relatively rich in random coil and extended strand, but transmembrane helices and signal peptides were not found. 4 MTs were mainly localized in cell nucleus (over 60%) and their cellular functions might have some relation to central intermediary metabolism. Multiple sequence alignment indicated relatively high identity (more than 52%) and short genetic distances (lower than 0.900) among 4 MT nucleotide sequences. Abundant genetic diversity and strong codon bias were found based on the halotype diversity, average number of nucleotide differences, nucleotide diversity, effective number of codons, codon bias index and scaled chisquare. Simultaneously, we deduced that 4 MT genes during molecular evolution were under positive selection. The present study might provide basis for further investigation of MTs molecular mechanisms and genetic laws.
Highlights
Metallothioneins (MTs) are a multigenic family of low-molecular weight, cysteine-rich, metal-binding proteins (7 metals/MT) that are widespread in animals, higher plants, eukaryotic microorganisms and some prokaryotes [1,2,3,4,5]
4 MTs were mainly localized in cell nucleus and their cellular functions might have some relation to central intermediary metabolism
Abundant genetic diversity and strong codon bias were found based on the halotype diversity, average number of nucleotide differences, nucleotide diversity, effective number of codons, codon bias index and scaled chi-square
Summary
Metallothioneins (MTs) are a multigenic family of low-molecular weight (ranging from 6 to 7 kDa), cysteine-rich (ranging from 20% to 33%), metal-binding proteins (7 metals/MT) that are widespread in animals, higher plants, eukaryotic microorganisms and some prokaryotes [1,2,3,4,5]. They are divided into three different classes on the basis of their cysteine content and structure. The results will give some theoretical foundations for molecular mechanisms and genetic laws of MT genes in fungi
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