OxyR: A molecular code for redox-related signaling
OxyR: A molecular code for redox-related signaling
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DOI：
10.1016/s0092-8674(02)00723-7
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发表时间：
2002-05-03
期刊：
影响因子：
64.5
通讯作者：
Stamler, JS
中科院分区：
文献类型：
--
作者：
Kim, SO;Merchant, K;Stamler, JS
氧化还原调节被认为是蛋白质中简单的开关（对应于还原和氧化状态）。使用转录因子OxyR作为模型，我们已经产生了，在体外，几个稳定的，翻译后修饰的单一监管硫醇（SH），包括S-NO，S-OH，和S-SG，并显示，每个发生在体内。OxyR的这些修饰形式具有转录活性，但在结构、协同性质、DNA结合亲和力和启动子活性方面不同。因此，OxyR可以将不同的氧化还原相关信号处理成不同的转录反应。更一般地说，我们的数据表明氧化还原控制的代码，通过该代码，变构蛋白可以subserve分级（合作）或最大（非合作）的反应，并通过该代码可以实现氧化还原相关信号的差分响应。
Redox regulation has been perceived as a simple on-off switch in proteins (corresponding to reduced and oxidized states). Using the transcription factor OxyR as a model, we have generated, in vitro, several stable, posttranslational modifications of the single regulatory thiol (SH), including S-NO, S-OH, and S-SG, and shown that each occurs in vivo. These modified forms of OxyR are transcriptionally active but differ in structure, cooperative properties, DNA binding affinity, and promoter activities. OxyR can thus process different redox-related signals into distinct transcriptional responses. More generally, our data suggest a code for redox control through which allosteric proteins can subserve either graded (cooperative) or maximal (noncooperative) responses, and through which differential responsivity to redox-related signals can be achieved.