RNase E cleavage in the atpE leader region of atpE/interferon-beta hybrid transcripts in Escherichia coli causes enhanced rates of mRNA decay

• Published in: The Journal of biological chemistry Vol. 266; no. 27; pp. 17880 - 17884
• Main Author: Gross, G.
• Format: Journal Article
• Language: English
• Published: United States American Society for Biochemistry and Molecular Biology 25.09.1991
• Subjects: Bacteriophage lambda - genetics; Base Sequence; Endoribonucleases - metabolism; Escherichia coli - genetics; Genes, Bacterial; Genes, Viral; Hydrolysis; Interferon Type I - genetics; Kinetics; Molecular Sequence Data; Promoter Regions, Genetic; Protein Biosynthesis; Protein Sorting Signals - genetics; RNA, Messenger - metabolism; Substrate Specificity; Transcription, Genetic
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/s0021-9258(18)55210-8

Chimeric transcripts containing the ribosome binding site of the Escherichia coli atpE gene and variants of the human structural interferon-beta gene are subject to RNase E processing in the 5'-untranslated atpE part of the transcripts. The absence of processing at two sites in the atpE leader-sequence caused by the RNase E deficiency in E. coli host N3431 leads to a considerable stabilization of the mRNA moiety. RNase E has originally been described as a processing enzyme for non-mRNAs such as precursor 5 S rRNA and RNA1, but cleavage mRNA substrates have also been reported. RNase E processing of the atpE gene leader sequence-containing transcripts leads to an increased rate of mRNA breakdown. The two RNase E-dependent processing sites in the atpE part of the mRNA transcripts exhibit some similarity to the other known RNase E processing sites. The influence of RNase E cleavage upon post-transcriptional regulation such as RNA stability and the efficiency of translational initiation is discussed.