PMID:10762247
| Citation |
Jiang, X, Diwa, A and Belasco, JG (2000) Regions of RNase E important for 5'-end-dependent RNA cleavage and autoregulated synthesis. J. Bacteriol. 182:2468-75 |
|---|---|
| Abstract |
RNase E is an important regulatory enzyme that plays a key role in RNA processing and degradation in Escherichia coli. Internal cleavage by this endonuclease is accelerated by the presence of a monophosphate at the RNA 5' end. Here we show that the preference of E. coli RNase E for 5'-monophosphorylated substrates is an intrinsic property of the catalytically active amino-terminal half of the enzyme and does not require the carboxy-terminal region. This property is shared by the related E. coli ribonuclease CafA (RNase G) and by a cyanobacterial RNase E homolog derived from Synechocystis, indicating that the 5'-end dependence of RNase E is a general characteristic of members of this ribonuclease family, including those from evolutionarily distant species. Although it is dispensable for 5'-end-dependent RNA cleavage, the carboxy-terminal half of RNase E significantly enhances the ability of this ribonuclease to autoregulate its synthesis in E. coli. Despite similarities in amino acid sequence and substrate specificity, CafA is unable to replace RNase E in sustaining E. coli cell growth or in regulating RNase E production, even when overproduced sixfold relative to wild-type RNase E levels. |
| Links | |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/metabolism; Base Sequence; Binding Sites; Cyanobacteria/enzymology; Cyanobacteria/genetics; Endoribonucleases/chemistry; Endoribonucleases/genetics; Endoribonucleases/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli Proteins; Genetic Complementation Test; Molecular Sequence Data; Nucleic Acid Conformation; RNA/biosynthesis; Structure-Activity Relationship |
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