A ribosomal polynucleotide phosphorylase in Pseudomonas aeruginosa

1962 ◽  
Vol 55 (1-2) ◽  
pp. 231-232 ◽  
Author(s):  
G.A. Strasdine ◽  
Loretta A. Hogg ◽  
J.J.R. Campbell
Author(s):  
Zheng Fan ◽  
Xiaolei Pan ◽  
Dan Wang ◽  
Ronghao Chen ◽  
Tongtong Fu ◽  
...  

Pseudomonas aeruginosa is an opportunistic pathogen that shows high intrinsic resistance to a variety of antibiotics. The MexX-MexY-OprM efflux pump plays an important role in the bacterial resistance to aminoglycoside antibiotics. Polynucleotide phosphorylase (PNPase) is a highly conserved exonuclease that plays important roles in RNA processing and bacterial response to environmental stresses. Previously, we demonstrated that PNPase controls the tolerance to fluoroquinolone antibiotics by influencing the production of pyocin in P. aeruginosa. In this study, we found that mutation of the PNPase coding gene (pnp) in P. aeruginosa increases the bacterial tolerance to aminoglycoside antibiotics. We further demonstrate that upregulation of the mexXY genes is responsible for the increased tolerance in the pnp mutant. Furthermore, our experimental results revealed that PNPase controls translation of the armZ mRNA through its 5′ untranslated region (5′-UTR). ArmZ had previously been shown to positively regulate the expression of mexXY. Therefore, our results revealed a novel role of PNPase in the regulation of armZ and subsequently the MexXY efflux pump.


1965 ◽  
Vol 11 (2) ◽  
pp. 337-344
Author(s):  
G. A. Strasdine ◽  
J. J. R. Campbell

Cell-free extracts of Pseudomonas aeruginosa formed ATP32from ADP and P32independent of concurrent oxidation. The ATP32resulted from the action of a coupled enzyme system involving a polynucleotide phosphorylase-mediated exchange reaction between ADP and P32and the subsequent action of adenylate kinase on ADP32yielding ATP32. Fractionation of the cell extract by differential centrifugation demonstrated that the polynucleotide phosphorylase of this organism was associated with a particulate cell fraction. The significance of this latter observation and the non-oxidative formation of ATP32is discussed with regard to studies of bacterial oxidative phosphorylation.


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