Escherichia coli K-12 substr. MG1655 Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateMacromolecule ReactionsPolynucleotide-ReactionsRNA-Reactions

EC Number:

Enzymes and Genes:
ribonuclease GInferred from experiment: rng

Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .

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 [Feng02]. The enzyme binds to monophosphorylated 5' ends of substrates but exhibits sequential cleavages in the 3' to 5' direction [Feng02] . 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 [Feng02]. 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 and EC

Citations: [Ehretsmann92, Cormack93, Vanzo98, Steege00, Callaghan03]

Gene-Reaction Schematic

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:

Created 20-Aug-2010 by Shearer A, SRI International


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

Feng02: 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

Steege00: Steege DA (2000). "Emerging features of mRNA decay in bacteria." RNA 6(8);1079-90. PMID: 10943888

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

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.5 on Fri Nov 27, 2015, BIOCYC13A.