Biochemical characterization and quantitative gene expression analysis of the multi-stress inducible metallothionein from Tetrahymena thermophila.

@article{Dondero2004BiochemicalCA,
  title={Biochemical characterization and quantitative gene expression analysis of the multi-stress inducible metallothionein from Tetrahymena thermophila.},
  author={Francesco Dondero and Maria Cavaletto and Anna Rita Ghezzi and Antonietta La Terza and Mohamed Banni and Aldo Viarengo},
  journal={Protist},
  year={2004},
  volume={155 2},
  pages={
          157-68
        }
}
A cadmium-binding protein with biochemical features of a metallothionein (MT) has been isolated and purified to homogeneity from the ciliate Tetrahymena thermophila. N-terminal sequencing revealed the posttranslational cleavage of the first two amino acids and, in general, a high degree of identity with known MTs from other ciliates. Matrix-Assisted Laser Desorption Ionization-Time of Flight Mass Spectrometry (MALDI-TOF MS) analysis of the apothionein revealed a molecular mass (16,763 Da… Expand
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TLDR
A novel cadmium-inducible metallothionein (MT) gene was cloned and sequenced from the ciliate Tetrahymena pigmentosa and the structure of Tpig-MT1 is different from the reported Cd-MT in T. pyriformis and T. thermophila. Expand
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TLDR
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TLDR
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The genome of the nematode Caenorhabditis elegans encodes for two multifunctional metal binding metallothioneins (MTs), CeMT-1 and CeMT-2. Here we applied qPCR to identify a transcriptionalExpand
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