Microscopy has localized tagged RNase E to the inner cytoplasmic membrane or a helical cytoskeletal structure closely associated with the inner layer.
[3] Although degradosome formation does not play a key role for E. coli growth,[4][5][6] the deletion of the C-terminal half has been found to decrease the rate of decay of some RNase E substrates.
[7][8] Ribonuclease E function in tetrameric conformation, which contains four subunits associate with each other to create a structure that looks like two scissors connected at the handle region.
The last subdomain of the RNase E catalytic site is DNase I, which is named for its conformational similarity to an endonuclease structure that cleaves double-stranded DNA.
In the maturation of rRNA precursor, the substrates for processing are not naked RNAs but somewhat incomplete, unmodified pre-rRNA-ribosomal protein complexes.
Both pre-16S and pre-23S rRNAs are excised from the primary RNA-protein complex by RNase III, which activates subsequent steps in rRNA maturation by generating 5' monophosphorylated cleavage products.
[17] The anchor of the RNase E to the 5′-monophosphorylated end of these substrates orients the enzyme for directional cleavages that occur in a processive mode.
The RNA is anchored primarily by the binding affinity of the 5′ sensor and oriented by the hydrophobic surface patch on the S1 subdomain.
When the RNA of interest is cleaved, and the products of the reaction are eventually released as RNase E returns to the open configuration.
Based on DNA sequence analysis, orthologs of E. coli RNase E were predicted to exist among dozens of evolutionarily different bacterial species.
In E. coli, the ribonuclease E enzyme plays an essential part in controlling cell viability by regulating RNA metabolism, such as the decay of most mRNAs and activates the processing of pre-tRNAs.