SPECTROSCOPIC CHARACTERIZATION OF THE COPPER(I)-THIOLATE CLUSTER IN THE DNA-BINDING DOMAIN OF YEAST ACE1 TRANSCRIPTION FACTOR

被引：15

作者：

CASASFINET, JR ^{[1
]}

HU, S ^{[1
]}

HAMER, D ^{[1
]}

KARPEL, RL ^{[1
]}

机构：

[1] NCI,BIOCHEM LAB,BETHESDA,MD 20892

来源：

FEBS LETTERS | 1991年 / 281卷 / 1-2期

关键词：

DNA-BINDING PROTEIN; METAL ION; LUMINESCENT COMPLEX;

D O I：

10.1016/0014-5793(91)80394-I

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A polypeptide containing the amino-terminal region of ACE1 (residues 1-122; 122*), the activator of yeast Cu-metallothionein gene transcription, shows charge-transfer and metal-centered UV absorption bands, and orange luminescence which are characteristic of Cu-cysteinyl thiolate cluster structures. These spectral features are abolished by the Cu(I) complexing agents CN- and diethyldithiocarbamate or exposure to acid, but not by the Cu(II) chelator, EDTA. Binding of the polypeptide to its specific DNA recognition site, but not to calf-thymus double-stranded DNA, induces quenching of its Tyr and Cu-S cluster luminescence emission. The CD spectrum is characteristic of a tightly folded structure that may be organized around the Cu cluster.

引用

页码：205 / 208

页数：4

共 9 条

[1]

BYRD J, 1988, J BIOL CHEM, V263, P6688

[2] COPPER AND THE ACE1 REGULATORY PROTEIN REVERSIBLY INDUCE YEAST METALLOTHIONEIN GENE-TRANSCRIPTION IN A MOUSE EXTRACT [J].