Literature summary for 3.1.26.3 extracted from

Carzaniga, T.; Deho, G.; Briani, F.
RNase III-independent autogenous regulation of Escherichia coli polynucleotide phosphorylase via translational repression (2015), J. Bacteriol., 197, 1931-1938 .

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A7Y0	-	-

Synonyms

Synonyms	Comment	Organism
RNase III	-	Escherichia coli

General Information

General Information	Comment	Organism
physiological function	the complex posttranscriptional regulation mechanism of the Escherichia coli pnp gene, which encodes the phosphorolytic exoribonuclease polynucleotide phosphorylase (PNPase), involves two endoribonucleases, namely, RNase III and RNase E, and PNPase itself, which thus autoregulates its own expression. Autogenous regulation of Escherichia coli PNPase via translational repression is RNase III-independent. The target of PNPase is a mature pnp mRNA previously processed at its 5' end by RNase III, rather than the primary pnp transcript (RNase III-dependent models). PNPase also regulates its own expression via a reversible RNase III-independent pathway acting upstream from the RNase III-dependent branch. This pathway requires the PNPase RNA binding domains KH and S1 but not its phosphorolytic activity. The RNase III-independent autoregulation of PNPase seem to occur at the level of translational repression, possibly by competition for pnp primary transcript between PNPase and the ribosomal protein S1	Escherichia coli

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Release 2023.1 (January 2023)