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. 1970 Sep;67(1):99–106. doi: 10.1073/pnas.67.1.99

Peptide Chain Termination with Mammalian Release Factor

J L Goldstein 1,2,*, A L Beaudet 1,2, C T Caskey 1,2
PMCID: PMC283173  PMID: 4917818

Abstract

We report a method for the in vitro study of peptide chain termination in mammals. A proteinaceous release factor has been isolated from rabbit reticulocyte extracts. This factor and a polyribonucleotide template containing the bases U and A stimulate the release of N-formylmethionine from mammalian [N-formylmethionyl-tRNAf·ribosome] intermediates. Our studies suggest that UAA is a terminator codon for mammalian cells.

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Selected References

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  1. ALLEN E. H., SCHWEET R. S. Synthesis of hemoglobin in a cell-free system. I. Properties of the complete system. J Biol Chem. 1962 Mar;237:760–767. [PubMed] [Google Scholar]
  2. Brown J. C., Smith A. E. Initiator codons in eukaryotes. Nature. 1970 May 16;226(5246):610–612. doi: 10.1038/226610a0. [DOI] [PubMed] [Google Scholar]
  3. Capecchi M. R., Klein H. A. Characterization of three proteins involved in polypeptide chain termination. Cold Spring Harb Symp Quant Biol. 1969;34:469–477. doi: 10.1101/sqb.1969.034.01.053. [DOI] [PubMed] [Google Scholar]
  4. Caskey C. T., Beaudet A., Nirenberg M. RNA codons and protein synthesis. 15. Dissimilar responses of mammalian and bacterial transfer RNA fractions to messenger RNA codons. J Mol Biol. 1968 Oct 14;37(1):99–118. doi: 10.1016/0022-2836(68)90076-4. [DOI] [PubMed] [Google Scholar]
  5. Caskey C. T., Redfield B., Weissbach H. Formylation of guinea pig liver methionyl-sRNA. Arch Biochem Biophys. 1967 Apr;120(1):119–123. doi: 10.1016/0003-9861(67)90605-4. [DOI] [PubMed] [Google Scholar]
  6. Caskey C. T., Tompkins R., Scolnick E., Caryk T., Nirenberg M. Sequential translation of trinucleotide codons for the initiation and termination of protein synthesis. Science. 1968 Oct 4;162(3849):135–138. doi: 10.1126/science.162.3849.135. [DOI] [PubMed] [Google Scholar]
  7. Caskey T., Scolnick E., Tompkins R., Goldstein J., Milman G. Peptide chain termination, codon, protein factor, and ribosomal requirements. Cold Spring Harb Symp Quant Biol. 1969;34:479–488. doi: 10.1101/sqb.1969.034.01.054. [DOI] [PubMed] [Google Scholar]
  8. Crick F. H. Codon--anticodon pairing: the wobble hypothesis. J Mol Biol. 1966 Aug;19(2):548–555. doi: 10.1016/s0022-2836(66)80022-0. [DOI] [PubMed] [Google Scholar]
  9. Fahnestock S., Neumann H., Shashoua V., Rich A. Ribosome-catalyzed ester formation. Biochemistry. 1970 Jun 9;9(12):2477–2483. doi: 10.1021/bi00814a013. [DOI] [PubMed] [Google Scholar]
  10. Garen A. Sense and nonsense in the genetic code. Three exceptional triplets can serve as both chain-terminating signals and amino acid codons. Science. 1968 Apr 12;160(3824):149–159. doi: 10.1126/science.160.3824.149. [DOI] [PubMed] [Google Scholar]
  11. Goldstein J., Milman G., Scolnick E., Caskey T. Peptide chain termination. VI. Purification and site of action of S. Proc Natl Acad Sci U S A. 1970 Feb;65(2):430–437. doi: 10.1073/pnas.65.2.430. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Gupta N. K. Studies on polynucleotides. LXXXIX. A study of amino acid incorporation in a reticulocyte cell-free protein-synthesizing system with polyribonucleotides with repeating nucleotide sequences used as messengers. J Biol Chem. 1968 Oct 10;243(19):4959–4965. [PubMed] [Google Scholar]
  13. Leder P., Bursztyn H. Initiation of protein synthesis II. A convenient assay for the ribosome-dependent synthesis of N-formyl-C14-methionylpuromycin. Biochem Biophys Res Commun. 1966 Oct 20;25(2):233–238. doi: 10.1016/0006-291x(66)90586-9. [DOI] [PubMed] [Google Scholar]
  14. Leder P., Singer M. F., Brimacombe R. L. Synthesis of trinucleoside diphosphates with polynucleotide phosphorylase. Biochemistry. 1965 Aug;4(8):1561–1567. doi: 10.1021/bi00884a015. [DOI] [PubMed] [Google Scholar]
  15. Lengyel P., Söll D. Mechanism of protein biosynthesis. Bacteriol Rev. 1969 Jun;33(2):264–301. doi: 10.1128/br.33.2.264-301.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Marshall R. E., Caskey C. T., Nirenberg M. Fine structure of RNA codewords recognized by bacterial, amphibian, and mammalian transfer RNA. Science. 1967 Feb 17;155(3764):820–826. doi: 10.1126/science.155.3764.820. [DOI] [PubMed] [Google Scholar]
  17. McKeehan W. L., Hardesty B. Purification and partial characterization of the aminoacyl transfer ribonucleic acid binding enzyme from rabbit reticulocytes. J Biol Chem. 1969 Aug 25;244(16):4330–4339. [PubMed] [Google Scholar]
  18. NIRENBERG M., LEDER P. RNA CODEWORDS AND PROTEIN SYNTHESIS. THE EFFECT OF TRINUCLEOTIDES UPON THE BINDING OF SRNA TO RIBOSOMES. Science. 1964 Sep 25;145(3639):1399–1407. doi: 10.1126/science.145.3639.1399. [DOI] [PubMed] [Google Scholar]
  19. SINGER M. F., GUSS J. K. The dependence of reactions catalyzed by polynucleotide phosphorylase on oligonucleotides. J Biol Chem. 1962 Jan;237:182–189. [PubMed] [Google Scholar]
  20. Scolnick E., Milman G., Rosman M., Caskey T. Transesterification by peptidyl transferase. Nature. 1970 Jan 10;225(5228):152–154. doi: 10.1038/225152a0. [DOI] [PubMed] [Google Scholar]
  21. Scolnick E., Tompkins R., Caskey T., Nirenberg M. Release factors differing in specificity for terminator codons. Proc Natl Acad Sci U S A. 1968 Oct;61(2):768–774. doi: 10.1073/pnas.61.2.768. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Scolnick E., Tompkins R., Caskey T., Nirenberg M. Release factors differing in specificity for terminator codons. Proc Natl Acad Sci U S A. 1968 Oct;61(2):768–774. doi: 10.1073/pnas.61.2.768. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Smith A. E., Marcker K. A. Cytoplasmic methionine transfer RNAs from eukaryotes. Nature. 1970 May 16;226(5246):607–610. doi: 10.1038/226607a0. [DOI] [PubMed] [Google Scholar]
  24. Tompkins R. K., Scolnick E. M., Caskey C. T. Peptide chain termination. VII. The ribosomal and release factor requirements for peptide release. Proc Natl Acad Sci U S A. 1970 Mar;65(3):702–708. doi: 10.1073/pnas.65.3.702. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Vazquez D., Battaner E., Neth R., Heller G., Monro R. E. The function of 80 S ribosomal subunits and effects of some antibiotics. Cold Spring Harb Symp Quant Biol. 1969;34:369–375. doi: 10.1101/sqb.1969.034.01.043. [DOI] [PubMed] [Google Scholar]
  26. Vogel Z., Zamir A., Elson D. The possible involvement of peptidyl transferase in the termination step of protein biosynthesis. Biochemistry. 1969 Dec;8(12):5161–5168. doi: 10.1021/bi00840a070. [DOI] [PubMed] [Google Scholar]

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