Phosphorylation of the conserved C-terminal domain of ribosomal P-proteins impairs the mode of interaction with plant toxins,FEBS Letters

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Phosphorylation of the conserved C-terminal domain of ribosomal P-proteins impairs the mode of interaction with plant toxins
FEBS Letters ( IF 3.0 ) Pub Date : 2021-07-30 , DOI: 10.1002/1873-3468.14170
Patrycja Horbowicz-Drożdżal ₁ , Karol Kamel ₂ , Sebastian Kmiecik ₃ , Lidia Borkiewicz ₄ , Nilgun E Tumer ₅ , Pang-Chui Shaw ₆ , Marek Tchórzewski ₁ , Przemysław Grela ₁

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The ribosome is subjected to post-translational modifications, including phosphorylation, that affect its biological activity. Among ribosomal elements, the P-proteins undergo phosphorylation within the C terminus, the element which interacts with trGTPases or ribosome-inactivating proteins (RIPs); however, the role of phosphorylation has never been elucidated. Here, we probed the function of phosphorylation on the interaction of P-proteins with RIPs using the ribosomal P1-P2 dimer. We determined the kinetic parameters of the interaction with the toxins using biolayer interferometry and microscale thermophoresis. The results present the first mechanistic insight into the function of P-protein phosphorylation, showing that introduction of a negative charge into the C terminus of P1-P2 proteins promotes α-helix formation and decreases the affinity of the P-proteins for the RIPs.

中文翻译：

核糖体 P 蛋白保守 C 端结构域的磷酸化损害与植物毒素的相互作用模式

核糖体受到影响其生物活性的翻译后修饰，包括磷酸化。在核糖体元件中，P 蛋白在 C 末端发生磷酸化，该元件与 trGTPases 或核糖体失活蛋白 (RIP) 相互作用；然而，磷酸化的作用从未被阐明。在这里，我们使用核糖体 P1-P2 二聚体探测了磷酸化对 P 蛋白与 RIP 相互作用的作用。我们使用生物层干涉仪和微型热泳法确定了与毒素相互作用的动力学参数。结果展示了对 P 蛋白磷酸化功能的第一个机制洞察，

更新日期：2021-09-13

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