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Literature summary for 3.1.26.12 extracted from

  • Caruthers, J.M.; Feng, Y.; McKay, D.B.; Cohen, S.N.
    Retention of core catalytic functions by a conserved minimal ribonuclease E peptide that lacks the domain required for tetramer formation (2006), J. Biol. Chem., 281, 27046-27051.
    View publication on PubMed
Search for more literature for 3.1.26.12

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged truncated enzyme mutants in Escherichia coli strain BL21(DE3), complementation of rne null mutation of Escherichia coli strain KSL2000 Haemophilus influenzae
expression of His-tagged truncated enzyme mutants in strain BL21(DE3), complementation of rne null mutation of strain KSL2000 Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information retention of core catalytic functions by a conserved minimal ribonuclease E peptide that lacks the domain required for tetramer formation, RNase E derivatives that are as short as 395 amino acid residues and that lack the Zn-link region shown previously to be essential for tetramer formation, residues 400-415, are catalytically active enzymes that retain the 5' to 3' scanning ability and cleavage site specificity characteristic of full-length RNase E and that also confer colony forming ability on rne null mutant bacteria. Further truncation leads to loss of these properties. A minimal catalytically active RNase E sequence proofs that a tetrameric quaternary structure is not required for RNase E to carry out its core enzymatic functions Escherichia coli
additional information retention of core catalytic functions by a conserved minimal ribonuclease E peptide that lacks the domain required for tetramer formation, RNase E derivatives that are as short as 395 amino acid residues and that lack the Zn-link region shown previously to be essential for tetramer formation, residues 400-415, are catalytically active enzymes that retain the 5' to 3' scanning ability and cleavage site specificity characteristic of full-length RNase E and that also confer colony forming ability on rne null mutant bacteria. Further truncation leads to loss of these properties. A minimal catalytically active RNase E sequence proofs that a tetrameric quaternary structure is not required for RNase E to carry out its core enzymatic functions Haemophilus influenzae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Escherichia coli
Mg2+
-
 Haemophilus influenzae

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 gene rne
-
Haemophilus influenzae P44443 gene rne
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged truncated enzyme mutants from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis and gel filtration Haemophilus influenzae
recombinant His-tagged truncated enzyme mutants from strain BL21(DE3) by nickel affinity chromatography, dialysis and gel filtration Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
BR30M + H2O endonucleolytic cleavage, a synthetic 30-mer oligoribonucleotide substrate containing 2'-O-methylated nucleotides at positions 16 and 17 Escherichia coli ?
-
 ?
BR30M + H2O endonucleolytic cleavage, a synthetic 30-mer oligoribonucleotide substrate containing 2'-O-methylated nucleotides at positions 16 and 17 Haemophilus influenzae ?
-
 ?

Synonyms

Synonyms Comment Organism
RNase E
-
 Escherichia coli
RNase E
-
 Haemophilus influenzae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Escherichia coli
30
-
 assay at Haemophilus influenzae

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
85
-
 inactivation Escherichia coli
85
-
 inactivation Haemophilus influenzae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Escherichia coli
8
-
 assay at Haemophilus influenzae