铜绿假单胞菌内源性呼吸过程中核糖体的酶促降解
Enzymatic Degradation of Ribosomes During Endogenous Respiration of Pseudomonas aeruginosa.
作者信息
Gronlund A F, Campbell J J
机构信息
Laboratory of Dairying, University of British Columbia, Vancouver, British Columbia, Canada.
出版信息
J Bacteriol. 1965 Jul;90(1):1-7. doi: 10.1128/jb.90.1.1-7.1965.
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 50S than 30S 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 70S ribosomes, but was active in low magnesium ion concentrations which allowed the 70S ribosome to dissociate. Polynucleotide phosphorylase was not solubilized after dissociation of the 70S particle, but remained firmly attached to the 50S and 30S ribosomes, the ribonucleic acid of which served as substrate.
格伦德，奥黛丽·F.（加拿大不列颠哥伦比亚省温哥华市英属哥伦比亚大学）和J.J.R.坎贝尔。铜绿假单胞菌内源呼吸过程中核糖体的酶促降解。《细菌学杂志》90:1 - 7。1965年。-通过沉降分析发现，铜绿假单胞菌的核糖体含量在内源呼吸过程中下降。在3小时的饥饿期内，50S核糖体比30S核糖体的降解程度更大。负责核糖体降解起始且存在于核糖体组分中的酶被鉴定为多核苷酸磷酸化酶。该酶在完整的70S核糖体中无活性，但在低镁离子浓度下有活性，低镁离子浓度会使70S核糖体解离。多核苷酸磷酸化酶在70S颗粒解离后未被溶解，而是仍牢固地附着在50S和30S核糖体上，其核糖核酸作为底物。
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