Prokaryotic enhancer-binding proteins reflect eukaryote-like modularity: the puzzle of nitrogen regulatory protein C.
Prokaryotic enhancer-binding proteins reflect eukaryote-like modularity: the puzzle of nitrogen regulatory protein C.
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原核增强子结合蛋白反映了真核生物的模块化：氮调节蛋白 C 之谜。
DOI：
10.1128/jb.175.14.4267-4273.1993
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发表时间：
1993
影响因子：
3.2
通讯作者：
Kustu,S
中科院分区：
文献类型：
--
作者：
North,AK;Klose,KE;Stedman,KM;Kustu,S
真核增强子结合蛋白通常是模块化设计的，因为它们由物理上可分离的结构域组成，这些结构域可以彼此独立地起作用（18,46,55）。详细的分析已经确定了参与特定DNA识别的区域和其他参与转录激活的区域。事实上，在许多情况下，将一种蛋白质的结构域与另一种蛋白质的结构域结合可以产生嵌合蛋白，该嵌合蛋白显示了每个亲本的预期功能特性（3,19,21,22）。如下所述，原核增强子结合蛋白家族的成员在结构上也是模块化的。然而，该家族的一个成员，肠道细菌的NTRC蛋白（氮调节蛋白C，也称为NRI）显然是一个例外。将NTRC的序列与其他激活剂的序列以及与反转刺激因子（FIS）的序列和结构进行比较，可能解释了NTRC令人困惑的特性。
Eukaryotic enhancer-binding proteins are often modular in design in that they are composed of physically separable domains that can function independently of one another (18, 46, 55). Detailed analyses have identified regions involved in specific DNA recognition and others involved in activation of transcription. In fact, in many instances, combining a domain from one protein with a second domain from another has produced a chimeric protein that demonstrates the expected functional properties of each parent (3, 19, 21, 22). As outlined below, members of a family of prokaryotic enhancer-binding proteins are also modular in structure. However, one member of the family, the NTRC protein (nitrogen regulatory protein C; also called NRI) of enteric bacteria, is apparently an exception. Comparison of the sequence of NTRC with that of other activators and with the sequence and structure of the factor for inversion stimula-tion (FIS) reveals a likely explanation for the puzzling properties of NTRC.