InterPro domain: IPR004659

Ribonuclease E and ribonuclease G are related enzymes that cleave a wide variety of RNAs [ 1 , 2 ]. In Escherichia coli, both enzymes have been shown to play a role in the maturation of the 5' end of 16S RNA [ 3 ]. RNase E is a major subunit the eubacterial degradosome - a large, multiprotein, multienzyme complex involved in RNA processing and degradation in E. coli and other proteobacteria [ 4 ]. These enzymes prefer 5'-monophosphorylated 5'-triphosphorylated substrates. The 5'-monophosphate-assisted cleavage requires at least 2 and preferably 3 or more unpaired 5'-terminal nucleotides [ 5 ].

1. Structure of Escherichia coli RNase E catalytic domain and implications for RNA turnover. Nature 437, 1187-91
2. Distinct Requirements for 5'-Monophosphate-assisted RNA Cleavage by Escherichia coli RNase E and RNase G. J Biol Chem 291, 5038-48
3. Escherichia coli cafA gene encodes a novel RNase, designated as RNase G, involved in processing of the 5' end of 16S rRNA. Biochem. Biophys. Res. Commun. 259, 483-8
4. The RNA degradosome: life in the fast lane of adaptive molecular evolution. Trends Biochem. Sci. 31, 359-65
5. Endonucleolytic cleavages by RNase E generate the mature 3' termini of the three proline tRNAs in Escherichia coli. Nucleic Acids Res 44, 6350-62