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Role of the ribosome‐associated protein PY in the cold‐shock response of Escherichia coli

机译:核糖体相关蛋白PY在大肠杆菌的冷休克反应中的作用

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AbstractProtein Y (PY) is an Escherichia coli cold-shock protein which has been proposed to be responsible for the repression of bulk protein synthesis during cold adaptation. Here, we present in vivo and in vitro data which clarify the role of PY and its mechanism of action. Deletion of yfiA, the gene encoding protein PY, demonstrates that this protein is dispensable for cold adaptation and is not responsible for the shutdown of bulk protein synthesis at the onset of the stress, although it is able to partially inhibit translation. In vitro assays reveal that the extent of PY inhibition changes with different mRNAs and that this inhibition is related to the capacity of PY of binding 30S subunits with a fairly strong association constant, thus stimulating the formation of 70S monomers. Furthermore, our data provide evidence that PY competes with the other ribosomal ligands for the binding to the 30S subunits. Overall these results suggest an alternative model to explain PY function during cold shock and to reconcile the inhibition caused by PY with the active translation observed for some mRNAs during cold shock.
机译:摘要蛋白质Y(​​PY)是一种大肠杆菌冷休克蛋白,已被提议负责冷适应过程中大块蛋白质合成的抑制。在这里,我们提供体内和体外数据,这些数据阐明了PY的作用及其作用机理。 yfiA(编码蛋白PY的基因)的缺失表明,该蛋白可用于冷适应,并且在应激发作时不负责批量蛋白质合成的关闭,尽管它能够部分抑制翻译。体外试验表明,PY抑制的程度随不同的mRNA改变,并且这种抑制与PY结合具有相当强的缔合常数的30S亚基的结合能力有关,从而刺激了70S单体的形成。此外,我们的数据提供了PY与其他核糖体配体竞争与30S亚基结合的证据。总的来说,这些结果提示了一种替代模型,该模型可以解释冷休克期间的PY功能,并使PY引起的抑制与冷休克期间某些mRNA的活性翻译相一致。

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