Rnase E/G-dependent degradation of metE mRNA, encoding methionine synthase, in corynebacterium glutamicum

Abstract

Corynebacterium glutamicum is used for the industrial production of various metabolites, includingL-glutamic acid andL-lysine. With the aim of understanding the post-transcriptional regulation of amino acid biosynthesis in this bacterium, we investigated the role of RNase E/G in the degradation of mRNAs encoding metabolic enzymes. In this study, we found that the cobalamin-independent methionine synthase MetE was overexpressed in ∆rneG mutant cells grown on various carbon sources. The level of metE mRNA was also approximately 6-to 10-fold higher in the ∆rneG mutant strain than in the wild-type strain. A rifampicin chase experiment showed that the half-life of metE mRNA was approximately 4.2 times longer in the ∆rneG mutant than in the wild-type strain. These results showed that RNase E/G is involved in the degradation of metE mRNA in C. glutamicum.