||RNase E is a bacterial ribonuclease that plays a role in the processing of ribosomal RNA (9S to 5S rRNA), the chemical degradation of bulk cellular RNA, the decay of specific regulatory, messenger and structural RNAs and the control of plasmid DNA replication . The enzyme binds to monophosphorylated 5′ ends of substrates but exhibits sequential cleavages in the 3′ to 5′ direction . 2′-O-Methyl nucleotide substitutions at RNase E binding sites do not prevent binding but do prevent cleavage of non-modified target sequences 5′ to that locus . In Escherichia coli, the enzyme is found in the RNA degradosome. The C-terminal half of the protein contains binding sites for the three other major degradosomal components, the DEAD-box RNA helicase Rh1B, enolase (EC 184.108.40.206) and polynucleotide phosphorylase (EC 220.127.116.11).
||Feng, Y., Vickers, T.A. and Cohen, S.N. The catalytic domain of RNase E shows inherent 3′ to 5′ directionality in cleavage site selection. Proc. Natl. Acad. Sci. USA 99 (2002) 14746–14751. [DOI] [PMID: 12417756]
||Ehretsmann, C.P., Carpousis, A.J. and Krisch, H.M. Specificity of Escherichia coli endoribonuclease RNase E: in vivo and in vitro analysis of mutants in a bacteriophage T4 mRNA processing site. Genes Dev. 6 (1992) 149–159. [DOI] [PMID: 1730408]
||Cormack, R.S., Genereaux, J.L. and Mackie, G.A. RNase E activity is conferred by a single polypeptide: overexpression, purification, and properties of the ams/rne/hmp1 gene product. Proc. Natl. Acad. Sci. USA 90 (1993) 9006–9010. [DOI] [PMID: 8415644]
||Vanzo, N.F., Li, Y.S., Py, B., Blum, E., Higgins, C.F., Raynal, L.C., Krisch, H.M. and Carpousis, A.J. Ribonuclease E organizes the protein interactions in the Escherichia coli RNA degradosome. Genes Dev. 12 (1998) 2770–2781. [DOI] [PMID: 9732274]
||Steege, D.A. Emerging features of mRNA decay in bacteria. RNA 6 (2000) 1079–1090. [PMID: 10943888]
||Callaghan, A.J., Grossmann, J.G., Redko, Y.U., Ilag, L.L., Moncrieffe, M.C., Symmons, M.F., Robinson, C.V., McDowall, K.J. and Luisi, B.F. Quaternary structure and catalytic activity of the Escherichia coli ribonuclease E amino-terminal catalytic domain. Biochemistry 42 (2003) 13848–13855. [DOI] [PMID: 14636052]