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Literature summary for 3.1.26.12 extracted from

  • Garrey, S.M.; Mackie, G.A.
    Roles of the 5-phosphate sensor domain in RNase E (2011), Mol. Microbiol., 80, 1613-1624.
    View publication on PubMed
Search for more literature for 3.1.26.12

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Protein Variants

Protein Variants Comment Organism
E R169Q mutant protein is strongly overexpressed with accumulation of proteolytic fragments Escherichia coli
additional information viable mutations affecting the 5'-phosphate sensor of RNase E, including R169Q or T170A, become lethal when combined with deletions removing part of the non-catalytic C-terminal domain of RNase E. Mutation of the phosphate sensor stabilizes the rpsT P1 mRNA as much as sixfold and slows the maturation of 16S rRNA. In contrast, the decay of other model mRNAs and the processing of several tRNA precursors are unaffected by mutations in the phosphate sensor Escherichia coli
additional information deletion of residues C-terminal to position 529 in the absence of other mutations still permit growth of cells. Deletion strain exhibits smaller colony size and reduced growth rates in liquid media. Additional shorter deletions spanning individual microdomains in the C-terminal scaffold region including the Arg-rich region, residues 608-644, the extended Arg-rich region with a putative coil-coil domain, residues 589-723, the RhlB binding site, residues 698–762, the enolase binding site, residues 833-850, or the PNPase binding site, residues 1021-1061, are viable, too Escherichia coli
R1269Q/DELTA530-1061 mutation is lethal Escherichia coli
R1269Q/DELTA589-1061 mutation is lethal Escherichia coli
R1269Q/DELTA730-1061 mutant is viable Escherichia coli
R169Q site-directed mutagensis, the viable mutation in the 5'-phosphate sensor of RNase E, becomes lethal in combination with deletions removing part of the non-catalytic C-terminal domain of RNase E. Loss of autoregulation in R169Q Escherichia coli
T170A site-directed mutagensis, the viable mutation in the 5'-phosphate sensor of RNase E, becomes lethal in combination with deletions removing part of the non-catalytic C-terminal domain of RNase E Escherichia coli
T170A/DELTA530-1061 mutant is viable, with small colony sizes Escherichia coli
T170A/DELTA589-1061 mutant is viable, with small colony sizes Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
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Escherichia coli P21513
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-

Synonyms

Synonyms Comment Organism
RNase E
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function the phosphate sensor domain in the enzyme is required for efficient autoregulation of RNase E synthesis. Impact of the 5'-sensor on mRNA stability, overview Escherichia coli
physiological function viable mutations affecting the 5'-phosphate sensor of RNase E, including R169Q or T170A, become lethal when combined with deletions removing part of the non-catalytic C-terminal domain of RNase E. The phosphate sensor is required for efficient autoregulation of RNase E synthesis as RNase E R169Q is strongly overexpressed with accumulation of proteolytic fragments. In addition, mutation of the phosphate sensorstabilizes the rpsT P1 mRNA as much as sixfold and slows the maturation of 16S rRNA. The decay of other model mRNAs and the processing of several tRNA precursors are unaffected by mutations in the phosphate sensor Escherichia coli