Szczypka M S, Thiele D J
Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor 48109-0606.
Mol Cell Biol. 1989 Feb;9(2):421-9. doi: 10.1128/mcb.9.2.421-429.1989.
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.
酿酒酵母的金属硫蛋白基因（CUP1）的铜诱导转录需要酵母的ACE1基因。克隆的ACE1基因序列预测了一个用于翻译225个氨基酸多肽的开放阅读框。该多肽的特征是富含半胱氨酸残基和带正电荷氨基酸的氨基末端区域。12个半胱氨酸中许多以Cys-X-Cys或Cys-X-X-Cys构型排列，这表明ACE1蛋白可能结合金属离子。ACE1蛋白的羧基末端区域不含半胱氨酸，但本质上高度酸性。双功能ACE1-β-半乳糖苷酶融合蛋白在酵母细胞核中积累的能力与ACE1在酵母金属硫蛋白基因的铜诱导转录调控中起直接作用的可能性一致。
