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. 1971 Aug;68(8):1805–1809. doi: 10.1073/pnas.68.8.1805

Interaction of Eukaryote Initiator Methionyl-tRNA with the Eukaryote Equivalent of Bacterial Elongation Factor T and Guanosine Triphosphate

Dietmar Richter *, Fritz Lipmann *,*, Adela Tarragó †, Jorge E Allende ‡
PMCID: PMC389297  PMID: 5288767

Abstract

The initiator tRNA, methionyl-tRNAiMet, of yeast and wheat germ forms relatively unstable ternary complexes with their corresponding elongation factors T and GTP. Such complexes can be demonstrated only with fast separation techniques such as Sephadex G-50 and Millipore filtration, but not with the slow Sephadex G-100 method, although both techniques yield stable ternary complexes with all other aminoacyl-tRNAs, including the internal Met-tRNAmMet. To bind yeast-initiating Met-tRNAiMet to ribosomes, initiation factors present in a ribosomal wash fraction from yeast are needed.

Keywords: yeast, wheat, Millipore filter, Sephadex

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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