|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Polynucleotide-Reactions → RNA-Reactions|
EC Number: 18.104.22.168
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.
Mass balance status: Balance undetermined; a substrate lacks a chemical formula
Enzyme Commission Primary Name: ribonuclease E
Enzyme Commission Synonyms: endoribonuclease E, RNase E, Rne protein
Enzyme Commission Summary:
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 [Feng02a]. The enzyme binds to monophosphorylated 5' ends of substrates but exhibits sequential cleavages in the 3' to 5' direction [Feng02a] . 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 [Feng02a]. 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, EC 22.214.171.124. and EC 126.96.36.199.
Callaghan03: Callaghan AJ, Grossmann JG, Redko YU, Ilag LL, Moncrieffe MC, Symmons MF, Robinson CV, McDowall KJ, Luisi BF (2003). "Quaternary structure and catalytic activity of the Escherichia coli ribonuclease E amino-terminal catalytic domain." Biochemistry 42(47);13848-55. PMID: 14636052
Cormack93: Cormack RS, Genereaux JL, Mackie GA (1993). "RNase E activity is conferred by a single polypeptide: overexpression, purification, and properties of the ams/rne/hmp1 gene product." Proc Natl Acad Sci U S A 90(19);9006-10. PMID: 8415644
Ehretsmann92: Ehretsmann CP, Carpousis AJ, Krisch HM (1992). "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(1);149-59. PMID: 1730408
Feng02a: Feng Y, Vickers TA, Cohen SN (2002). "The catalytic domain of RNase E shows inherent 3' to 5' directionality in cleavage site selection." Proc Natl Acad Sci U S A 99(23);14746-51. PMID: 12417756
Vanzo98: Vanzo NF, Li YS, Py B, Blum E, Higgins CF, Raynal LC, Krisch HM, Carpousis AJ (1998). "Ribonuclease E organizes the protein interactions in the Escherichia coli RNA degradosome." Genes Dev 12(17);2770-81. PMID: 9732274
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