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首页> 外文期刊>Molecular and Cellular Biology >Dephosphorylation of S6 and expression of the heat shock response in Drosophila melanogaster.
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Dephosphorylation of S6 and expression of the heat shock response in Drosophila melanogaster.

机译：果蝇S6的去磷酸化和热休克反应的表达。

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A basic ribosomal phosphoprotein of 30,000 molecular weight was rapidly dephosphorylated in cultured Drosophila melanogaster cells heat shocked at 37 degrees C. The protein was associated with the 40S ribosomal subunit and had an electrophoretic mobility similar to that of purified rat liver protein S6 on basic two-dimensional polyacrylamide gels as well as a similar partial proteolysis peptide map. In logarithmically growing cultures, this D. melanogaster S6 protein appeared to have a single phosphorylated species consisting of 30 to 40% of the total cellular S6. Thus, the nearly complete dephosphorylation of this protein observed in heat shock involves a large fraction of the cellular S6. The significance of this dephosphorylation in the expression of the heat shock response was investigated by examining the phosphorylation status of S6 in recovery from heat shock and in response to chemical inducers of the heat shock response. During recovery from a 30-min heat shock, the recovery of normal protein synthesis was almost complete in 2 to 4 hr, whereas there was no significant rephosphorylation of S6 for 8 h. Two chemical inducers of the heat shock response, canavanine and sodium arsenite, induced the synthesis of heat shock proteins in D. melanogaster cells. Sodium arsenite also caused an inhibition of normal protein synthesis similar to that observed in heat shock. Neither agent, however, caused significant dephosphorylation of S6. These results suggest that the dephosphorylation of S6, although invariably observed in heat-shocked cells, may in some cases be dissociated from both the induction of heat shock protein synthesis and the turnoff of normal protein synthesis which occur in a heat shock response.
机译：在37摄氏度热休克的果蝇果蝇细胞中，分子量为30,000的碱性核糖体磷蛋白被快速去磷酸化。该蛋白与40S核糖体亚基缔合，其电泳迁移率与纯化的大鼠肝脏蛋白质S6相似，在基本的两个维聚丙烯酰胺凝胶以及类似的部分蛋白水解肽图。在对数生长的培养物中，黑腹果蝇D. S6蛋白似乎具有单个磷酸化物质，占总细胞S6的30％至40％。因此，在热激中观察到的该蛋白质的几乎完全脱磷酸涉及细胞S6的很大一部分。通过检查S6在从热激中恢复以及响应于热激反应的化学诱导物的磷酸化状态，研究了这种去磷酸化在热激反应表达中的重要性。从30分钟的热休克恢复过程中，正常蛋白质合成的恢复在2-4小时内几乎完成，而S6在8小时内没有明显的再磷酸化。两种热刺激反应的化学诱导剂，黄花碱和亚砷酸钠，诱导了D. melanogaster细胞中热激蛋白的合成。亚砷酸钠也引起对正常蛋白质合成的抑制，类似于在热激中观察到的抑制作用。但是，两种试剂均未引起S6的显着去磷酸化。这些结果表明，尽管在热激细胞中总是观察到S6的去磷酸化，但是在某些情况下，S6的去磷酸化可能与热激蛋白合成的诱导和在热激反应中发生的正常蛋白合成的关闭均分离。

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