Association and dissociation of the GlnK-AmtB complex in response to cellular nitrogen status can occur in the absence of GlnK post-translational modification.
Association and dissociation of the GlnK-AmtB complex in response to cellular nitrogen status can occur in the absence of GlnK post-translational modification.
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DOI：
10.3389/fmicb.2014.00731
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发表时间：
2014
影响因子：
5.2
通讯作者：
Merrick M
中科院分区：
文献类型：
--
作者：
Radchenko MV;Thornton J;Merrick M
PII蛋白在控制细菌和古细菌的氮代谢中起着关键作用，也存在于植物的质体中。PII蛋白控制多种酶、转录因子和膜转运蛋白的活性，其调控作用是通过与其靶点直接相互作用实现的。许多，但绝不是全部，PII蛋白受到蛋白质t环内残基翻译后修饰的影响。蛋白质的修饰状态受细胞氮状态的影响，过去认为这通过控制与靶蛋白的相互作用来调节PII活性。然而，PII蛋白响应细胞氮状态的基本能力已被证明依赖于关键效应分子，ATP， ADP和2-氧葡萄糖酸盐的结合，这使人们对翻译后修饰的确切作用产生了疑问。在这项研究中，我们使用大肠杆菌PII蛋白GlnK来检测翻译后修饰（尿苷化）对GlnK与其同源靶点氨通道蛋白AmtB之间相互作用的影响。我们比较了野生型GlnK和一种不能尿苷化的变异蛋白GlnKTyr51Ala与AmtB的相互作用。该分析是在体内和体外进行的，结果表明GlnK - amtb复合物的结合和解离并不依赖于GlnK的尿苷化状态。然而，我们的体内研究表明，GlnK的翻译后修饰确实会影响其与AmtB相互作用的动力学。
PII proteins are pivotal players in the control of nitrogen metabolism in bacteria and archaea, and are also found in the plastids of plants. PII proteins control the activities of a diverse range of enzymes, transcription factors and membrane transport proteins, and their regulatory effect is achieved by direct interaction with their target. Many, but by no means all, PII proteins are subject to post-translational modification of a residue within the T-loop of the protein. The protein’s modification state is influenced by the cellular nitrogen status and in the past this has been considered to regulate PII activity by controlling interaction with target proteins. However, the fundamental ability of PII proteins to respond to the cellular nitrogen status has been shown to be dependent on binding of key effector molecules, ATP, ADP, and 2-oxoglutarate which brings into question the precise role of post-translational modification. In this study we have used the Escherichia coli PII protein GlnK to examine the influence of post-translational modification (uridylylation) on the interaction between GlnK and its cognate target the ammonia channel protein AmtB. We have compared the interaction with AmtB of wild-type GlnK and a variant protein, GlnKTyr51Ala, that cannot be uridylylated. This analysis was carried out both in vivo and in vitro and showed that association and dissociation of the GlnK–AmtB complex is not dependent on the uridylylation state of GlnK. However, our in vivo studies show that post-translational modification of GlnK does influence the dynamics of its interaction with AmtB.
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影响因子：
4.8
作者：
Radchenko, Martha V.;Thornton, Jeremy;Merrick, Mike
通讯作者：
Merrick, Mike
影响因子：
3.6
作者：
Hesketh, A;Fink, D;Engels, A
通讯作者：
Engels, A
DOI：
10.1073/pnas.0610348104
发表时间：
2007-01-23
影响因子：
11.1
作者：
Conroy, Matthew J.;Durand, Anne;Merrick, Mike
通讯作者：
Merrick, Mike
影响因子：
3.6
作者：
Strösser, J;Lüdke, A;Burkovski, A
通讯作者：
Burkovski, A
影响因子：
11.4
作者：
Coutts, G;Thomas, G;Merrick, M
通讯作者：
Merrick, M