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Literature summary for 4.6.1.24 extracted from

  • Chung, D.H.; Min, Z.; Wang, B.C.; Kushner, S.R.
    Single amino acid changes in the predicted RNase H domain of Escherichia coli RNase G lead to complementation of RNase E deletion mutants (2010), RNA, 16, 1371-1385.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene rng, overexpression of wild-type rng and of mutant rngs in rne-1 or rneD1018 alleles mutant strains Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information two distinct spontaneously derived single amino acid substitutions within the predicted RNase H domain of RNase G, generate the rng-219 and rng-248 alleles, which complement the rne mutant strains. Domain swaps between RNase E and RNase G generate proteins that do not complement RNase E deficiency Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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gene rng
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Synonyms

Synonyms Comment Organism
RNase G
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Escherichia coli

General Information

General Information Comment Organism
metabolism distinct roles of RNase E and RNase G in mRNA decay and tRNA processing, overview Escherichia coli
additional information neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneD1018 alleles, encoding RNase E, even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the predicted RNase H domain of RNase G, generating the rng-219 and rng-248 alleles, result in complementation of the growth defect associated with various RNase E mutants. Complementation of the growth defect associated with RNase E-deficient strains is dependent on the intracellular level of the Rng-219 and Rng-248 proteins Escherichia coli
physiological function RNase G is involved in the maturation of the 5' terminus of 16S rRNA, the processing of a few tRNAs, and the initiation of decay of a limited number of mRNAs but is not required for cell viability and cannot substitute for RNase E under normal physiological conditions Escherichia coli