Decreased activity of peptide-elongation factors after treatment with cholesterol esterase.
1. Peptide-elongation factors were purified from rat liver and treated with cholesterol esterase and phospholipase A2 immobilized on Sepharose 4B. 2. Binding of L-[3H]-phenylalanyl-tRNA to 40S ribosomal subunits was decreased by approx. 70% and to polyribosomes by 30% in the presence of the binding factor incubated with cholesterol esterase. Treatment of this factor with immobilized phospholipase A2 decreased the binding to smaller ribosomal subunits by only about 15%. 3. Poly(U)-dependent phenylalanine polymerization by ribosomal subunits was decreased to approx. 30% of its original value by treatment of both elongation factors with cholesterol esterase. 4. The normal activity of esterase-treated elongation factor in both the binding reaction and peptide-elongation assay was fully recovered by the addition of cholesteryl 14-methyl-hexadecanoate. 5. Different classes of lipids present in peptide-elongation factor 1 have apparently different functions. Whereas phospholipids are required to maintain the strcture of heavy aggregates of this factor, the presence of cholesteryl 14-methylhexadecanoate is obviously necessary for the normal function of peptide-elongation factors.
D000818:Animals; D002265:Carboxylic Ester Hydrolases / Q000494:pharmacology*; D002788:Cholesterol Esters / Q000378:metabolism / Q000494:pharmacology; D005260:Female; D066298:In Vitro Techniques; D008099:Liver / Q000378:metabolism; D008297:Male; D010441:Peptide Chain Elongation, Translational / Q000187:drug effects; D010445:Peptide Elongation Factors; D010740:Phospholipases / Q000494:pharmacology; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism; D051381:Rats; D012270:Ribosomes / Q000378:metabolism; D002787:Sterol Esterase / Q000494:pharmacology*
D002788:Cholesterol Esters; D010445:Peptide Elongation Factors; D012346:RNA, Transfer, Amino Acyl; C005463:carcinolipin; D010740:Phospholipases; D002265:Carboxylic Ester Hydrolases; D002787:Sterol Esterase
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