title: Decreased activity of peptide-elongation factors after treatment with cholesterol esterase.
abstract: 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.
mesh_terms: 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*
chemical_list: D002788:Cholesterol Esters; D010445:Peptide Elongation Factors; D012346:RNA, Transfer, Amino Acyl; C005463:carcinolipin; D010740:Phospholipases; D002265:Carboxylic Ester Hydrolases; D002787:Sterol Esterase
references.citation: Proc Natl Acad Sci U S A. 1973 Dec;70(12):3282-6
references.pmid: 4519622
references.citation: Arch Biochem Biophys. 1974 Apr 2;161(2):709-12
references.pmid: 4839057
references.citation: Biochem J. 1972 Mar;126(5):1225-9
references.pmid: 5073734
references.citation: FEBS Lett. 1970 Sep 24;10(2):121-124
references.pmid: 11945372
references.citation: Arch Biochem Biophys. 1976 Jun;174(2):603-12
references.pmid: 1230010
references.citation: Biochem J. 1969 Dec;115(5):873-80
references.pmid: 5360722
references.citation: Methods Enzymol. 1974;30:354-67
references.pmid: 4605104
references.citation: Biochem J. 1968 Mar;107(2):129-34
references.pmid: 5689245
references.citation: Prog Biochem Pharmacol. 1975;10:197-226
references.pmid: 1093207
references.citation: Acta Biol Med Ger. 1974;33(5-6):929-32
references.pmid: 4619954
references.citation: Biochem J. 1974 Feb;138(2):147-54
references.pmid: 4595729
references.citation: Proc Natl Acad Sci U S A. 1972 May;69(5):1249-52
references.pmid: 4556458
references.citation: J Mol Biol. 1971 Aug 28;60(1):113-22
references.pmid: 5572099
references.citation: Biochem J. 1971 Aug;123(5):959-66
references.pmid: 5124397
references.citation: Proc Natl Acad Sci U S A. 1971 Feb;68(2):390-4
references.pmid: 5277091
references.citation: Biochemistry. 1971 Dec 21;10(26):4906-12
references.pmid: 5134535