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Literature summary for 3.1.26.12 extracted from

  • Walsh, A.P.; Tock, M.R.; Mallen, M.H.; Kaberdin, V.R.; von Gabain, A.; McDowall, K.J.
    Cleavage of poly(A) tails on the 3'-end of RNA by ribonuclease E of Escherichia coli (2001), Nucleic Acids Res., 29, 1864-1871.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.26.12

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged full-length wild-type RNase E and His-tagged N-terminal ribonucleolytic domain RTD-RNase E, residues 1-498, in strain BL21(DE3) Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
additional information the enzyme is not inhibitable by commercially available RNase A inhibitor Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information the enzyme is part of the RNA degradosome multi-protein complex, which also contains enolase, RhlB, and PNPase Escherichia coli
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli BRL2288
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native RNA degradosome from strain BRL2288, recombinant His-tagged full-length wild-type RNase E and His-tagged N-terminal ribonucleolytic domain RTD-RNase E from strain BL21(DE3) by metal affinity chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
RNA + H2O the enzyme or its isolated N-terminal catalytic domain cleave poly(A) tails on the 3' end of RNA substrates, the RNA degradosome cleaves 3' poly(A) tails of RNA irrespective of the 5' phosphorylation status, while the purified RNase E shows high preference for 5'-monophosphorylated RNA substrates, and low activity with 5'-triphosphate RNA, N-terminal ribonucleolytic domain RTD-RNase E is the catalytic domain and sufficient for activity Escherichia coli ?
-
 ?
RNA + H2O the enzyme or its isolated N-terminal catalytic domain cleave poly(A) tails on the 3' end of RNA substrates, the RNA degradosome cleaves 3' poly(A) tails of RNA irrespective of the 5' phosphorylation status, while the purified RNase E shows high preference for 5'-monophosphorylated RNA substrates, and low activity with 5'-triphosphate RNA, N-terminal ribonucleolytic domain RTD-RNase E is the catalytic domain and sufficient for activity Escherichia coli BRL2288 ?
-
 ?

Subunits

Subunits Comment Organism
More N-terminal ribonucleolytic domain RTD-RNase E is the catalytic domain and sufficient for activity Escherichia coli

Synonyms

Synonyms Comment Organism
ribonuclease E
-
 Escherichia coli
RNase E
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
 assay at Escherichia coli