A cysteine-rich nuclear protein activates yeast metallothionein gene transcription.


Journal Article

The ACE1 gene of the yeast Saccharomyces cerevisiae is required for copper-inducible transcription of the metallothionein gene (CUP1). The sequence of the cloned ACE1 gene predicted an open reading frame for translation of a 225-amino-acid polypeptide. This polypeptide was characterized by an amino-terminal half rich in cysteine residues and positively charged amino acids. The arrangement of many of the 12 cysteines in the configuration Cys-X-Cys or Cys-X-X-Cys suggested that the ACE1 protein may bind metal ions. The carboxyl-terminal half of the ACE1 protein was devoid of cysteines but was highly acidic in nature. The ability of a bifunctional ACE1-beta-galactosidase fusion protein to accumulate in yeast cell nuclei was consistent with the possibility that ACE1 plays a direct role in the regulation of copper-inducible transcription of the yeast metallothionein gene.

Full Text

Duke Authors

Cited Authors

  • Szczypka, MS; Thiele, DJ

Published Date

  • February 1989

Published In

Volume / Issue

  • 9 / 2

Start / End Page

  • 421 - 429

PubMed ID

  • 2651899

Pubmed Central ID

  • 2651899

International Standard Serial Number (ISSN)

  • 0270-7306

Digital Object Identifier (DOI)

  • 10.1128/mcb.9.2.421


  • eng

Conference Location

  • United States