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Literature summary for 3.1.13.1 extracted from

  • Song, L.; Wang, G.; Malhotra, A.; Deutscher, M.P.; Liang, W.
    Reversible acetylation on Lys501 regulates the activity of RNase II (2016), Nucleic Acids Res., 44, 1979-1988 .
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
recombinant overexpression of His-tagged wild-type non-acetylated and acetylated RNase II and of FLAG-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) lacking Pka or CobB Escherichia coli

Protein Variants

Protein Variants Comment Organism
K501Q site-directed mutagenesis, mutation of Lys501 results in up to 80% reduction in acetylation of RNase II Escherichia coli
K501R site-directed mutagenesis, mutation of Lys501 results in up to 80% reduction in acetylation of RNase II Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
additional information acetylation at enzyme residue Lys501 affects binding of the substrate and decreases the catalytic activity of RNase II Escherichia coli
nicotinamide NAM Escherichia coli
trichostatin A TSA Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, no degradation of the RNA occurs in the absence of Mg2+ Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P30850
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
acetylation residue Lys501 is acetylated in RNase II. This modification, reversibly controlled by the acetyltransferase Pka and the deacetylase CobB, a SIRT family deacetylase, affects binding of the substrate and thus decreases the catalytic activity of RNase II. Acetylation can regulate the activity of a bacterial ribonuclease. Lys501 is the major site of acetylation in this enzyme, but some other lysine residues in RNase II are also susceptible to acetylation. After enzyme inhibitor nicotinamide treatment, the acetylation level of RNase II increases 2-3fold in both wild-type and mutant strains. Inactivation of CobB increased the acetylation of wild-type RNase II Escherichia coli

Purification (Commentary)

Purification (Comment) Organism
recombinant His- or FLAG-tagged wild-type non-acetylated and acetylated and mutants from Escherichia coli strain BL21(DE3) by affinity chromatography Escherichia coli

Synonyms

Synonyms Comment Organism
RNase II
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

pH Optimum

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

General Information

General Information Comment Organism
metabolism role for RNase II Lys501 acetylation in modulating cell growth during stress conditions Escherichia coli
physiological function RNase II is a 3' to 5' processive exoribonuclease and is the major hydrolytic enzyme in Escherichia coli accounting for about 90% of the total activity. Acetylation of residue Lys501 in RNase II, reversibly controlled by the acetyltransferase Pka and the deacetylase CobB, affects binding of the substrate and decreases the catalytic activity of RNase II. As a consequence, the steady-state level of target RNAs of RNase II may be altered in the cells. Under conditions of slowed growth, the acetylation level of RNase II is elevated and the activity of RNase II decreases, emphasizing the importance of this regulatory process Escherichia coli