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Degradation of initiator tRNA(Met) by Xrn1/2 via its accumulation in the nucleus of heat-treated HeLa cells

机译:Xrn1 / 2通过其在热处理过的HeLa细胞核中的积累而降解启动子tRNA(Met)

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摘要

Stress response mechanisms that modulate the dynamics of tRNA degradation and accumulation from the cytoplasm to the nucleus have been studied in yeast, the rat hepatoma and human cells. In the current study, we investigated tRNA degradation and accumulation in HeLa cells under various forms of stress. We found that initiator tRNA(Met) (tRNA(iMet)) was specifically degraded under heat stress. Two exonucleases, Xrn1 and Xrn2, are involved in the degradation of tRNA(iMet) in the cytoplasm and the nucleus, respectively. In addition to degradation, we observed accumulation of tRNA(iMet) in the nucleus. We also found that the mammalian target of rapamycin (mTOR), which regulates tRNA trafficking in yeast, is partially phosphorylated at Ser2448 in the presence of rapamycin and/or during heat stress. Our results suggest phosphorylation of mTOR may correlate with accumulation of tRNA(iMet) in heat-treated HeLa cells.
机译:已经在酵母,大鼠肝癌和人类细胞中研究了调节tRNA降解和从细胞质到细胞核积累的动力学的应激反应机制。在当前的研究中,我们研究了在各种形式的压力下,HeLa细胞中tRNA的降解和积累。我们发现,启动子tRNA(Met)(tRNA(iMet))在热应激下被特异性降解。两个外切核酸酶Xrn1和Xrn2分别参与细胞质和细胞核中tRNA(iMet)的降解。除降解外,我们还观察到了tRNA(iMet)在细胞核中的积累。我们还发现,在雷帕霉素存在下和/或在热应激期间,调节​​酵母中tRNA转运的雷帕霉素(mTOR)哺乳动物靶标在Ser2448处被部分磷酸化。我们的结果表明,mTOR的磷酸化可能与热处理过的HeLa细胞中tRNA(iMet)的积累有关。

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