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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >THE AMINO-TERMINAL DOMAIN OF THE PROKARYOTIC ENHANCER-BINDING PROTEIN XYLR IS A SPECIFIC INTRAMOLECULAR REPRESSOR
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THE AMINO-TERMINAL DOMAIN OF THE PROKARYOTIC ENHANCER-BINDING PROTEIN XYLR IS A SPECIFIC INTRAMOLECULAR REPRESSOR

机译：原核增强剂结合蛋白XYLR的氨基酸末端域是一种特定的分子内阻遏物

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摘要

The mechanism under which the signal-reception amino terminal portion (A domain) of the prokaryotic enhancer-binding protein XylR controls the activity of the regulator has been investigated through complementation tests in vivo, in which the various protein segments were produced as independent polypeptides, Separate expression of the A domain repressed the otherwise constitutive activity of a truncated derivative of XylR deleted of its A domain (XylR Delta A). Such inhibition was not released by m-xylene, the natural inducer of the system, Repression caused by the A domain was specific for XylR because it did not affect activation of the sigma(54) promoter PnifH by a derivative of its cognate regulator, NifA, deleted of its own A domain, The A domain was also unable to repress the activity of a NifA-XylR hybrid protein resulting from fusing two-thirds of the central domain of NifA to the carboxyl-terminal third of XylR, which includes its DNA-binding domain. The inhibitory effect caused by the A domain of XylR on XylR Delta A seems, therefore, to result from specific interactions in trans between the two truncated proteins and not from mere hindering of an activating surface. [References: 30]
机译：已通过体内互补试验研究了原核增强子结合蛋白XylR的信号接收氨基末端部分（A结构域）控制调节子活性的机制，其中各种蛋白质片段均作为独立的多肽产生， A结构域的单独表达抑制了其A结构域缺失的XylR截短衍生物的原本构性活性（XylR Delta A）。这种抑制作用不是由系统的自然诱导物间二甲苯释放的，由A结构域引起的阻遏是XylR特有的，因为它不影响其同源调节剂NifA激活sigma（54）启动子PnifH的激活。 ，其自身的A结构域被删除，该A结构域也无法抑制NifA-XylR杂合蛋白的活性，这是由于将NifA的三分之二的中央结构域融合到XylR的羧基末端三分之一（包括其DNA）而产生的绑定域。因此，XylR的A结构域对XylR Delta A的抑制作用似乎是由于两个截短蛋白之间的反式特异性相互作用所致，而不是仅仅阻碍了活化表面。 [参考：30]

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