Post-translational modification of P II signal transduction proteins.
Post-translational modification of P II signal transduction proteins.
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DOI：
10.3389/fmicb.2014.00763
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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：
Merrick M
PII蛋白是自然界分布最广泛的信号转导蛋白家族之一。它们在细菌和古菌的氮代谢控制中起着关键作用，也存在于植物的质体中。非常值得注意的是，PII蛋白控制着一系列酶、转录因子和膜运输蛋白的活性，在所有已知的情况下，它们都是通过与靶标直接相互作用来实现调节作用的。变形杆菌和放线菌中的PII蛋白分别通过尿苷基化或腺苷基化进行翻译后修饰，而在一些蓝藻中，它们可以通过磷酸化修饰。在所有这些情况下，蛋白质的修饰状态都受到细胞氮状态的影响，并被认为调节其活性。然而，在许多生物体中，没有证据表明PII蛋白被修饰，事实上，这些蛋白对细胞氮状态的反应能力从根本上独立于翻译后修饰。在这篇综述中，我们结合最近的研究探讨了翻译后修饰在PII蛋白中的作用。
The PII proteins constitute one of the most widely distributed families of signal transduction proteins in nature. They are pivotal players in the control of nitrogen metabolism in bacteria and archaea, and are also found in the plastids of plants. Quite remarkably PII proteins control the activities of a diverse range of enzymes, transcription factors and membrane transport proteins, and in all known cases they achieve their regulatory effect by direct interaction with their target. PII proteins in the Proteobacteria and the Actinobacteria are subject to post-translational modification by uridylylation or adenylylation respectively, whilst in some Cyanobacteria they can be modified by phosphorylation. In all these cases the protein’s modification state is influenced by the cellular nitrogen status and is thought to regulate its activity. However, in many organisms there is no evidence for modification of PII proteins and indeed the ability of these proteins to respond to the cellular nitrogen status is fundamentally independent of post-translational modification. In this review we explore the role of post-translational modification in PII proteins in the light of recent studies.
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影响因子：
2.9
作者：
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通讯作者：
Ninfa, Alexander J.
影响因子：
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作者：
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通讯作者：
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作者：
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DOI：
10.1073/pnas.0610348104
发表时间：
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影响因子：
11.1
作者：
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通讯作者：
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