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Literature summary for 3.1.26.12 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

Protein Variants

Protein Variants Comment Organism
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 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. Construction of rneD1018/rng-219 and rneD1018/rng-248 double mutants. Domain swaps between RNase E and RNase G generate proteins that do not complement RNase E deficiency Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pre-tRNACys + H2O Escherichia coli
-
tRNACys + 3'-leader of tRNA
-
?
pre-tRNAHis + H2O Escherichia coli
-
tRNAHis + 3'-leader of tRNA
-
?
pre-tRNAPro + H2O Escherichia coli
-
tRNAPro + 3'-leader of tRNA
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli
-
gene rne
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pre-tRNACys + H2O
-
Escherichia coli tRNACys + 3'-leader of tRNA
-
?
pre-tRNAHis + H2O
-
Escherichia coli tRNAHis + 3'-leader of tRNA
-
?
pre-tRNAPro + H2O
-
Escherichia coli tRNAPro + 3'-leader of tRNA
-
?

Synonyms

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

General Information

General Information Comment Organism
malfunction absence of RNase E differentially affects the decay of specific mRNAs. 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 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 Escherichia coli
metabolism the endoribonuclease RNase E of Escherichia coli is an essential enzyme that plays a major role in all aspects of RNA metabolism Escherichia coli
physiological function RNase E is essential for cell viability and plays a major role in mRNA decay, rRNA maturation, tRNA processing, and a variety of other aspects of RNA metabolism. Maturation of tRNACys, tRNAHis, and tRNAPro but not tRNAAsn is completely dependent on RNase E Escherichia coli
physiological function neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with RNase E deletion mutants 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, suggesting that this region of the two proteins may help distinguish their in vivo biological activities Escherichia coli