Department of Molecular Biology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Lublin, Poland.
Biological and Chemical Research Centre, Faculty of Chemistry, University of Warsaw, Warsaw, Poland.
FEBS Lett. 2020 Sep;594(18):3002-3019. doi: 10.1002/1873-3468.13885. Epub 2020 Jul 31.
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.
uL10 蛋白是核糖体 P stalk 的主要成分，通过与 rRNA 的相互作用将整个 stalk 锚定在核糖体上。P stalk 是 GTPase 相关中心 (GAC) 的核心，对于核糖体生物发生和核糖体翻译活性至关重要。所有 P stalk 蛋白（uL10、P1 和 P2）在其 C 末端发生磷酸化。在这里，我们表明 uL10 具有多个磷酸化位点，也映射在 N 末端 rRNA 结合结构域内。我们的结果表明，在 uL10 的 N 末端引入负电荷会损害其与核糖体的结合。这些发现表明 uL10 N 端磷酸化具有调节潜力，控制 uL10 与核糖体的相互作用，并可能控制 GAC 的活性。
