Affiliation:
1. Laboratory of Dairying, University of British Columbia, Vancouver, British Columbia, Canada
Abstract
Gronlund, Audrey
F. (University of British Columbia, Vancouver, B.C., Canada),
and J. J. R. Campbell
. Enzymatic degradation of ribosomes during endogenous respiration of
Pseudomonas aeruginosa
. J. Bacteriol.
90:
1–7. 1965.—From sedimentation analyses it was found that the ribosomal content of
Pseudomonas aeruginosa
decreased during endogenous respiration. A greater degree of degradation of 50
S
than 30
S
ribosomes 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 70
S
ribosomes, but was active in low magnesium ion concentrations which allowed the 70
S
ribosome to dissociate. Polynucleotide phosphorylase was not solubilized after dissociation of the 70
S
particle, but remained firmly attached to the 50
S
and 30
S
ribosomes, the ribonucleic acid of which served as substrate.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
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