Functional analysis of Escherichia coli RNase G and its application for construction of protein expression system

点击翻译按钮获取中文摘要

In order to elucidate the regulatory mechanism of mRNA stability by the Escherichia coli endoribonuclease RNase G, action of RNase G on adhE mRNA was investigated. As a result, it was revealed that adhE mRNA cleaved by RNase G at -17 was rapidly degraded while one cleaved by RNase III at -31 was translated. It was found that RNase G mutant strains overproduced pyruvate because of increased stability of mRNAs encoding glycolysis enzymes. According to this finding, a new method for fermentative production of pyruvate and valine was established. It was found that processing of the ftsZ mRNA encoding the essential cell division protein FtsZ was an essential reaction of RNase E required for cell viability. In the RNase E mutant cells, translation of the unprocessed ftsZ mRNA was inhibited by the RNA-binding protein Hfq. For these results, it is suggested that mRNA stability control by endoribonucleases is widely involved in the regulatory mechanism of gene expression in E.coli.