首页> 外文期刊>Journal of Molecular Biology >Both Temperature and Medium Composition Regulate RNase E Processing Efficiency of the rpsO mRNA Coding for Ribosomal Protein S15 of Escherichia coli.
【24h】

Both Temperature and Medium Composition Regulate RNase E Processing Efficiency of the rpsO mRNA Coding for Ribosomal Protein S15 of Escherichia coli.

机译:温度和培养基组成均调节大肠杆菌核糖体蛋白S15的rpsO mRNA编码的RNase E加工效率。

获取原文
获取原文并翻译 | 示例
           

摘要

Cleavage by RNase E is believed to be the rate-limiting step in the degradation of many RNAs. These cleavages are modulated by 5' end-phosphorylation, folding and translation of the mRNA in question. Here, we present data suggesting that these cleavages are also regulated by environmental conditions. We report that rpsO mRNA, 15 minutes after a shift to 44 degrees C, is stabilized in cells grown in minimal medium. This stabilization is correlated with a reduction in the efficiency of the RNase E cleavage which initiates its decay. We also observe the appearance of RNA fragments previously detected following RNase E inactivation and a defect in the adaptation of RNase E concentration. These observations, coupled to the fact that RNase E overproduction slightly reduces the accumulation of the rpsO mRNA, suggest that this stabilization is caused in part by a limitation in RNase E concentration. An increase in the steady-state level of rpsT mRNA is also observed following a shift to 44 degrees C in minimal medium; however, processing of the 9 S rRNA precursor is not affected under these conditions. We thus propose that RNase E concentration changes in the cell in response to environmental conditions and that these changes can selectively affect the processing and the stability of individual mRNAs. Our data also indicate that the efficiency of cleavage of the rpsO mRNA by RNase E is modified by other factor(s) which remain to be identified. (c) 2002 Elsevier Science Ltd.
机译:RNase E的切割被认为是许多RNA降解中的限速步骤。这些裂解是通过所讨论的mRNA的5'末端磷酸化,折叠和翻译来调节的。在这里,我们提出的数据表明这些裂解也受到环境条件的调节。我们报告说,在移至44摄氏度后15分钟,rpsO mRNA在基本培养基中生长的细胞中稳定。这种稳定与引起其衰变的RNase E切割效率降低相关。我们还观察到先前在RNase E失活后检测到的RNA片段的出现以及RNase E浓度适应性的缺陷。这些观察结果与RNase E过量生产会略微降低rpsO mRNA的积累有关,这表明这种稳定化部分是由于RNase E浓度的限制所致。在基本培养基中移至44摄氏度后,还观察到rpsT mRNA稳态水平的增加。但是,在这些条件下,9 S rRNA前体的加工不受影响。因此,我们建议响应环境条件,细胞中RNase E的浓度发生变化,并且这些变化可以选择性地影响单个mRNA的加工和稳定性。我们的数据还表明,RNase E切割rpsO mRNA的效率受到其他因素的修饰,这些因素尚待确定。 (c)2002爱思唯尔科学有限公司。

著录项

相似文献

  • 外文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号