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. 1972 Sep;69(9):2451–2455. doi: 10.1073/pnas.69.9.2451

Polypeptide Chain Initiation and Stepwise Elongation with Artemia Ribosomes and Factors*

Ralph P McCroskey 1, Michael Zasloff 1, Severo Ochoa 1
PMCID: PMC426963  PMID: 4560686

Abstract

The supernatant initiation factor from Artemia salina embryos promotes, besides the AUG-dependent binding of fMet-tRNAf, the poly(U)-dependent binding of N-acetylPhe-tRNA to 40S ribosomal subunits; the bound N-acylaminoacyl-tRNA reacts directly with puromycin upon addition of 60S subunits. Both the binding reaction and the synthesis of N-acylaminoacyl-puromycin occur in the absence of GTP or other ribonucleoside triphosphates. To a smaller extent, the factor also mediates the 40S ribosomal binding of Met-tRNAf and Phe-tRNA; in this case, the bound aminoacyl-tRNA is less reactive with puromycin. After the poly(U)- and supernatant factor-dependent binding of N-acetylPhe-tRNA to 40S subunits at low Mg2+ concentration, binding of a second aminoacyl-tRNA (Phe-tRNA), with ensuing formation of the first peptide bond, is dependent upon the addition of the 60S subunit, elongation factor EF-1, and GTP. Further growth of the polypeptide chain requires translocation and is, therefore, dependent upon the addition of elongation factor EF-2. As with the Escherichia coli system, once requirements for translation of the third codon have been met, no further additions are necessary for elongation of a peptide chain.

Keywords: Artemia salina, embryos, cysts, brine-shrimp eggs, poly(U)

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Selected References

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