Literature summary for 2.7.7.8 extracted from

Cameron, T.A.; Matz, L.M.; Sinha, D.; De Lay, N.R.
Polynucleotide phosphorylase promotes the stability and function of Hfq-binding sRNAs by degrading target mRNA-derived fragments (2019), Nucleic Acids Res., 47, 8821-8837 .

Search for more literature for 2.7.7.8

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P05055	-	-

General Information

General Information	Comment	Organism
physiological function	polynucleotide phosphorylase contributes to the degradation of specific short mRNA fragments, the majority of which bind RNA chaperone Hfq and are derived from targets of sRNAs. The mRNA-derived fragments accumulate in the absence of polynucleotide phosphorylase or its exoribonuclease activity and interact with polynucleotide phosphorylase. Mutations in chaperone Hfq or in the seed pairing region of some sRNAs eliminate the requirement of polynucleotide phosphorylase for their stability	Escherichia coli

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)