NITRIC-OXIDE DESTROYS ZINC-SULFUR CLUSTERS INDUCING ZINC RELEASE FROM METALLOTHIONEIN AND INHIBITION OF THE ZINC FINGER-TYPE YEAST TRANSCRIPTION ACTIVATOR LAC9
NITRIC-OXIDE DESTROYS ZINC-SULFUR CLUSTERS INDUCING ZINC RELEASE FROM METALLOTHIONEIN AND INHIBITION OF THE ZINC FINGER-TYPE YEAST TRANSCRIPTION ACTIVATOR LAC9
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DOI：
10.1006/bbrc.1994.1564
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发表时间：
1994-04-29
影响因子：
3.1
通讯作者：
KOLBBACHOFEN, V
中科院分区：
文献类型：
--
作者：
KRONCKE, KD;FEHSEL, K;KOLBBACHOFEN, V
由s -亚硝基半胱氨酸生成或作为气体应用的一氧化氮通过sh基团氧化介导金属离子从Zn2+/Cd2+络合蛋白金属硫蛋白中释放出来。时间依赖的s -亚硝基化和随后的金属硫蛋白二硫形成证明。此外，一氧化氮抑制含有锌指状DNA结合域的酵母转录因子LAC9的DNA结合活性。这些结果表明，一氧化氮与蛋白质中的锌-硫簇相互作用并破坏它们。(C) 1994学术出版社，Inc.
Nitric oxide, generated from S-nitrosocysteine or applied as gas mediates metal ion release from the Zn2+/Cd2+-complexing protein metallothionein via oxidation of SH-groups. Time-dependent S-nitrosylation and subsequent disulfide formation of metallothionein are demonstrated. Furthermore, nitric oxide inhibits DNA binding activity of the yeast transcription factor LAC9 containing a zinc finger like DNA binding domain. These results show that nitric oxide interacts with and destroys zinc-sulfur clusters in proteins. (C) 1994 Academic Press, Inc.