Enzymatic Degradation of Ribosomes During Endogenous Respiration ofPseudomonas aeruginosa

Publisher Website
Google Scholar
Abstract
Gronlund, AudreyF. (University of British Columbia, Vancouver, B.C., Canada),and J. J. R. Campbell. Enzymatic degradation of ribosomes during endogenous respiration ofPseudomonas aeruginosa. J. Bacteriol.90:1–7. 1965.—From sedimentation analyses it was found that the ribosomal content ofPseudomonas aeruginosadecreased during endogenous respiration. A greater degree of degradation of 50Sthan 30Sribosomes occurred during the 3-hr starvation period. The enzyme responsible for the initiation of ribosome degradation and present in the ribosome fraction was identified as polynucleotide phosphorylase. The enzyme was inactive in intact 70Sribosomes, but was active in low magnesium ion concentrations which allowed the 70Sribosome to dissociate. Polynucleotide phosphorylase was not solubilized after dissociation of the 70Sparticle, but remained firmly attached to the 50Sand 30Sribosomes, the ribonucleic acid of which served as substrate.