EC Number   |
Natural Substrates |
|---|
   2.7.7.8 | more |
enzyme is involved in tuning the expression of virulence genes and bacterial fitness during infection |
| 2.7.7.8 | more |
enzyme may play a role in excluding oxidized forms of RNA from the translation mechanism |
| 2.7.7.8 | more |
suppression of Rho-dependent transcription termination within the enzyme gene and its restoration by enzyme protein is an autogenous regulation circuit that modulates enzyme gene expression during cold acclimation |
| 2.7.7.8 | more |
PNPase is one of the main exonucleolytic activities involved in RNA turnover and is widely conserved, but PNPase does not seem to be essential for growth, if the organisms are not subjected to special conditions, such as low temperature, transcriptional regulation, overview |
| 2.7.7.8 | more |
enzyme affects the expression and activity of the type III secretion system by distinct mechanisms. the RNA-binding subdomain S1-dependent effect on type III secretion system involves an RNA intermediate |
| 2.7.7.8 | more |
polynucleotide phosphorylase is essential for growth at low temperatures, while polymerization activity is not essential. RNase PH domains 1 and 2 of polynucleotide phosphorylase are important for its cold shock function, suggesting that the RNase activity of the enzyme is critical for its essential function at low temperature. Its polymerization activity is dispensable in its cold shock function. The RNase R , which is cold inducible, cannot complement the cold shock function of PNPase |
| 2.7.7.8 | more |
polynucleotide phosphorylase is involved in protecting cells and limiting damaged RNA under oxidative conditions |
| 2.7.7.8 | more |
polyribonucleotide phosphorylase-mediated degradation is a major regulatory event controlling the levels of sRNAs, namely stationary phase regulators MicA and RybB, that are required for the accurate expression of outer membrane proteins. Degradation by PNPase surpasses the effect of endonucleolytic cleavages by RNase E. Polyribonucleotide phosphorylase is an important enzyme in the growth phase adaptation to stationary phase |
| 2.7.7.8 | more |
regulates its own expression at the level of mRNA stability and translation |
| 2.7.7.8 | more |
the apoptosis-inducing activity of polynucleotide phosphorylase is mediated by activation of double-stranded RNAdependent protein kinase. Activation of RNA-dependent protein kinase by polynucleotide phosphorylase precedes phosphorylation of eukaryotic initiation factor-2A and induction of growth arrest and DNA damage-inducible gene 153, GADD153, that culminates in the shutdown of protein synthesis and apoptosis. Activation of RNA-dependent protein kinase by polynucleotide phosphorylase also instigates down-regulation of the antiapoptotic protein Bcl-xL |
