Replacement of All α-domain lysines with glutamates reduces metallothionein detoxification function

Chris W. Cody, P. C. Huang

Research output: Contribution to journalArticlepeer-review

Abstract

Mammalian metallothioneins (MTs) possess eight highly conserved lysine residues, including three in each of two metal binding domains. We used site-directed mutagenesis to replace these intradomain lysines in Chinese hamster ovary MT2 with glutamic acid and/or glutamine. These mutant MTs were expressed in a metal sensitive yeast host. One mutant which had all three lysines in the α-domain replaced by glutamates (K43,51,56E) exhibited a reduced ability, relative to native MT, to protect yeast transformants against otherwise toxic levels of cadmium. This triply substituted mutant also exhibited anomalous migration on a non-denaturing gel relative to wild type MT and other MT lysine mutants, suggesting that the intradomain lysines are important in maintaining the conformational integrity of MT.

Original languageEnglish (US)
Pages (from-to)954-959
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume202
Issue number2
DOIs
StatePublished - Jul 29 1994

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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