Phosphorylation of the N‐terminal domain of ribosomal P‐stalk protein uL10 governs its association with the ribosome,FEBS Letters

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Phosphorylation of the N‐terminal domain of ribosomal P‐stalk protein uL10 governs its association with the ribosome
FEBS Letters ( IF 3.0 ) Pub Date : 2020-07-31 , DOI: 10.1002/1873-3468.13885
Kamil Filipek ₁ , Barbara Michalec-Wawiórka ₁ , Aleksandra Boguszewska ₁ , Sebastian Kmiecik ₂ , Marek Tchórzewski ₁

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The uL10 protein is the main constituent of the ribosomal P‐stalk, anchoring the whole stalk to the ribosome through interactions with rRNA. The P‐stalk is the core of the GTPase‐associated center (GAC), a critical element for ribosome biogenesis and ribosome translational activity. All P‐stalk proteins (uL10, P1, and P2) undergo phosphorylation within their C termini. Here, we show that uL10 has multiple phosphorylation sites, mapped also within the N‐terminal rRNA‐binding domain. Our results reveal that the introduction of a negative charge within the N terminus of uL10 impairs its association with the ribosome. These findings demonstrate that uL10 N‐terminal phosphorylation has regulatory potential governing the uL10 interaction with the ribosome and may control the activity of GAC.

中文翻译：

核糖体 P-stalk 蛋白 uL10 N 末端结构域的磷酸化控制其与核糖体的关联

uL10 蛋白是核糖体 P 茎的主要成分，通过与 rRNA 的相互作用将整个茎固定在核糖体上。P-stalk 是 GTPase 相关中心 (GAC) 的核心，是核糖体生物发生和核糖体翻译活性的关键元素。所有 P-stalk 蛋白（uL10、P1 和 P2）都在其 C 末端发生磷酸化。在这里，我们显示 uL10 具有多个磷酸化位点，也位于 N 端 rRNA 结合域内。我们的结果表明，在 uL10 的 N 末端引入负电荷会削弱其与核糖体的关联。这些发现表明 uL10 N 端磷酸化具有调控 uL10 与核糖体相互作用的调节潜力，并可能控制 GAC 的活性。

更新日期：2020-07-31

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