Mechanism of Transcriptional Activation by NtrC
Mechanism of Transcriptional Activation by NtrC
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NtrC 转录激活机制
DOI：
--
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发表时间：
1995
期刊：
影响因子：
--
通讯作者：
S. Kustu
中科院分区：
文献类型：
--
作者：
S. Porter;A. North;S. Kustu
在氮调节蛋白C（NtrC）的情况下，核苷酸水解和转录激活都依赖于蛋白质的N-末端受体结构域（也称为其调节结构域）中天冬氨酸残基的磷酸化。在这一章中，作者回顾了来自肠道细菌的NtrC蛋白在溶液中是二聚体，必须形成适当的寡聚体才能水解核苷酸并激活转录的证据。因为已知NtrC的N-末端受体结构域的磷酸化增加寡聚化，所以磷酸化对NtrC功能的影响可能是对寡聚化的影响的结果。最近的实验室证据表明，NtrC的寡聚化决定簇位于其中央激活结构域。NtrC功能的研究已经通过使用两种工具来促进：NtrC的突变形式和glnA增强子的衍生物。NtrC必须在其受体结构域磷酸化以水解ATP并激活转录。磷酸化刺激NtrC的寡聚化，而寡聚化又是ATP水解和转录激活所需的。由于NtrC的磷酸化接收器结构域发挥积极作用，因此可能需要适当的寡聚化：通过蛋白质水解或基因工程去除该结构域并不能取代磷酸化。然而，未磷酸化的蛋白质基本上不能ATP水解或转录激活，即使与增强子结合。
In the case of nitrogen regulatory protein C (NtrC), both nucleotide hydrolysis and transcriptional activation depend on phosphorylation of an aspartate residue in the N-terminal receiver domain of the protein (also called its regulatory domain). In this chapter, the authors review the evidence that the NtrC protein from enteric bacteria, which is a dimer in solution, must form an appropriate oligomer to hydrolyze nucleotide and activate transcription. Because phosphorylation of the N-terminal receiver domain of NtrC is known to increase oligomerization, effects of phosphorylation on NtrC function may be a consequence of effects on oligomerization. Recent evidence from the laboratory indicates that oligomerization determinants of NtrC are located in its central activation domain. Studies of NtrC function have been facilitated by the use of two sorts of tools: mutant forms of NtrC and derivatives of the glnA enhancer. NtrC must be phosphorylated in its receiver domain to hydrolyze ATP and activate transcription. Phosphorylation stimulates the oligomerization of NtrC, and oligomerization is, in turn, required for ATP hydrolysis and transcriptional activation. Because the phosphorylated receiver domain of NtrC functions positively, it is presumably needed for appropriate oligomerization: removing this domain by proteolysis or genetic engineering does not substitute for phosphorylation. However, the unphosphorylated protein is essentially incapable of ATP hydrolysis or transcriptional activation, even when bound to the enhancer.
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原核转录增强子和增强子结合蛋白。
影响因子：
13.8
作者：
Kustu,S;North,AK;Weiss,DS
通讯作者：
Weiss,DS
影响因子：
5.6
作者：
KLOSE, KE;WEISS, DS;KUSTU, S
通讯作者：
KUSTU, S
DOI：
10.1073/pnas.85.14.4976
发表时间：
1988-07-01
影响因子：
11.1
作者：
KEENER, J;KUSTU, S
通讯作者：
KUSTU, S
影响因子：
5.6
作者：
FLASHNER, Y;WEISS, DS;KUSTU, S
通讯作者：
KUSTU, S
肠道细菌氮调节蛋白 NTRC 二聚化的主要决定因素在于其羧基末端结构域。
影响因子：
5.6
作者：
Klose,KE;North,AK;Stedman,KM;Kustu,S
通讯作者：
Kustu,S