Characterization of the copper-thiolate cluster in yeast metallothionein and two truncated mutants.

@article{Byrd1988CharacterizationOT,
  title={Characterization of the copper-thiolate cluster in yeast metallothionein and two truncated mutants.},
  author={J P Byrd and Raymond M. Berger and David R McMillin and Cynthia F. Wright and Dean H. Hamer and Dennis R Winge},
  journal={The Journal of biological chemistry},
  year={1988},
  volume={263 14},
  pages={6688-94}
}
Cu-metallothionein was purified from Saccharomyces cerevisiae harboring plasmids containing mutated CUP1 metallothionein genes resulting in deletions at the carboxy-terminal end of the polypeptide. The truncated polypeptides are recovered as polypeptides of 35 and 48 residues in length. The Cu-S cluster in the wild-type metallothionein and the two truncates were characterized. The truncated proteins, designated T35 and T48, contain 4 and 2 fewer cysteinyl residues, respectively, compared to the… CONTINUE READING

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