Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.7.8 extracted from

  • De Lay, N.; Gottesman, S.
    Role of polynucleotide phosphorylase in sRNA function in Escherichia coli (2011), RNA, 17, 1172-1189.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
C1310T mutation invovled in sRNA regulation defects Escherichia coli
C277T mutation invovled in sRNA regulation defects Escherichia coli
C943T mutation invovled in sRNA regulation defects Escherichia coli
G1307A mutation invovled in sRNA regulation defects Escherichia coli
G1466A mutation invovled in sRNA regulation defects Escherichia coli
additional information genetic selection and screen for mutants defective in the post-transcriptional regulation of gene expression by sRNAs, i.e. CyaR, SgrS, and RyhB. Each of the pnp mutations isolated, as well as a pnp deletion, are transduced into strain DJ624, overview. The defect in sRNA regulation caused by the pnp mutations is independent of Hfq. While Hfq does not appear to be limiting, it seems possible that lack of PNPase leads to inactivation of Hfq Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
gene pnp
-
Escherichia coli MG1193
-
gene pnp
-

Synonyms

Synonyms Comment Organism
PNPase
-
Escherichia coli
polynucleotide phosphorylase
-
Escherichia coli

General Information

General Information Comment Organism
malfunction loss-of-function mutations in pnp result in a decreased stability of several sRNAs including RyhB, SgrS, and CyaR and also decrease both the negative and positive regulation by sRNAs. The defect in stability of CyaR and in negative and positive regulation are suppressed by deletion mutations in RNase E. Lack of sRNA-mediated regulation in the absence of an active form of PNPase is due to the rapid turnover of sRNA resulting from an increase in RNase E activity and/or an increase in access of other ribonucleases to sRNAs. The defect in sRNA regulation caused by the pnp mutations is independent of Hfq. While Hfq does not appear to be limiting, it seems possible that lack of PNPase leads to inactivation of Hfq Escherichia coli