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Literature summary for 3.1.26.12 extracted from

  • Ikeda, Y.; Yagi, M.; Morita, T.; Aiba, H.
    Hfq binding at RhlB-recognition region of RNase E is crucial for the rapid degradation of target mRNAs mediated by sRNAs in Escherichia coli (2011), Mol. Microbiol., 79, 419-432.
    View publication on PubMed
Search for more literature for 3.1.26.12

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of FLAG-tagged truncation mutants Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information the scaffold region of RNase E to bind Hfq can be deleted up to residue 750 without losing the ability to cause the rapid degradation of target mRNAs mediated by Hfq/sRNAs. The truncated RNase E750 can still bind to Hfq although the truncation significantly reduces the Hfq-binding ability. Deletion of the 702-750 region greatly impairs the ability of RNase E to cause the degradation of ptsG mRNA Escherichia coli
additional information The scaffold region of RNase E can be deleted up to residue 750 without losing the ability to cause the rapid degradation of target mRNAs mediated by Hfq/sRNAs. The truncated RNase E750 can still bind to Hfq although the truncation significantly reduces the Hfq-binding ability. Deletion of the 702-750 region greatly impairs the ability of RNase E to cause the degradation of ptsG mRNA. A polypeptide corresponding to the scaffold region binds to Hfq without the help of RNA. Overexpression of RhlB partially inhibits the Hfq binding to RNase E and the rapid degradation of ptsG mRNA Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
additional information overexpression of RhlB partially inhibits the Hfq binding to RNase E and the rapid degradation of ptsG mRNA Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information RNA chaperon Hfq along with Hfq-binding sRNAs stably binds to RNase E in Escherichia coli. The role of the Hfq-RNase E interaction is to recruit RNase E to target mRNAs of sRNAs resulting in the rapid degradation of the mRNA-sRNA hybrid. The scaffold region of RNase E can be deleted up to residue 750 without losing the ability to cause the rapid degradation of target mRNAs mediated by Hfq/sRNAs. The truncated RNase E750 can still bind to Hfq although the truncation significantly reduces the Hfq-binding ability. Deletion of the 702-50 region greatly impairs the ability of RNase E to cause the degradation of ptsG mRNA. A polypeptide corresponding to the scaffold region binds to Hfq without the help of RNA. Overexpression of RhlB partially inhibits the Hfq binding to RNase E and the rapid degradation of ptsG mRNA Escherichia coli ?
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 ?

Synonyms

Synonyms Comment Organism
RNase E
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 Escherichia coli

General Information

General Information Comment Organism
physiological function RNase E is responsible for the functional interaction with Hfq to cause the sRNA-mediated destabilization of target mRNAs. the RNA chaperon Hfq along with Hfq-binding sRNAs stably binds to RNase E in Escherichia coli. The role of the Hfq-RNase E interaction is to recruit RNase E to target mRNAs of sRNAs resulting in the rapid degradation of the mRNA-sRNA hybrid. The C-terminal scaffold region of RNase E is responsible for the interaction with Hfq. Mutational interaction analysis, overview Escherichia coli