Influence of Guanine Nucleotides and Elongation Factors on Interaction of Release Factors with the Ribosome
Open accessAbstract
Release of formylmethionine from the reticulocyte ribosomal substrate, f[ 3 H]Met-tRNA·ribosome, is promoted by reticulocyte release factor (RF). The initial rate of this reaction is stimulated by GTP but inhibited by GDPCP. Formation of an RF·UA[ 3 H]A 2 ·ribosome complex is a measure of the binding of reticulocyte RF to the ribosome, and the recovery of this complex is increased by GDPCP and, to a lesser extent, GTP. These studies suggest that GTP is involved in the initial association of RF with the ribosome and that hydrolysis of the γ-phosphate of the guanine nucleotide is required at a subsequent rate-limiting step. The ribosomal-dependent fMet-tRNA hydrolysis and GTPase activities of reticulocyte RF are inhibited when elongation factor (EF)-2 is bound to the respective ribosomal substrate in the presence of fusidic acid and GDP. When EF-G is bound to the f[ 3 H]Met-tRNA·AUG·ribosome substrate with fusidic acid and GDP, the fMet-tRNA hydrolysis activity of Escherichia coli RF-1 and RF-2 is also inhibited. The binding of reticulocyte RF and E. coli RF-1 or RF-2 to their respective ribosomes is prevented when fusidic acid·EF-2/EF-G·GDP·ribosome complexes are used.
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The three stop codons differ substantially in termination efficiency and accuracy in eukaryotes.
“In fact, multiple lines of evidence suggest much difference in termination efficiency and accuracy among the three stop codons.”
From Detailed Dissection and Critical Evaluation of the Pfizer/BioNTech and Moderna mRNA Vaccines (2021) · cites this paper as [64]
The Results report that reticulocyte release factor recognizes all three stop codons and that a higher concentration of UAGA was needed for complete competition in a ribosome-binding assay. That is limited evidence of a difference in codon recognition, not a demonstration that termination efficiency or accuracy differs substantially among the three codons in eukaryotes. The paper also notes contamination of the UAGA preparation. (LLM, conf=0.78)
Experimental — accuracy not yet measuredUAA (especially UAAA) is more efficient than other stop signals.
“These studies suggest that UAA (especially UAAA) is more efficient than other stop signals.”
From Detailed Dissection and Critical Evaluation of the Pfizer/BioNTech and Moderna mRNA Vaccines (2021) · cites this paper as [64]
The Results (Fig. 3; page unavailable) report that UAAA, UAGA, and UGAA all competed for release-factor binding, but that UAGA required a higher concentration for complete competition. This supports an advantage for UAAA over UAGA in that binding assay, not the broader claim that UAA or UAAA is more efficient than all other stop signals at termination. (LLM, conf=0.83)
Experimental — accuracy not yet measuredThe binding affinity to eRF1 is in the order of UAA > UGA and UAG, suggesting that UAA is a more efficient stop codon than the other two.
“First, the binding affinity to eRF1 is in the order of UAA > UGA and UAG [63,64], suggesting that UAA is a more efficient stop codon than the other two.”
From Detailed Dissection and Critical Evaluation of the Pfizer/BioNTech and Moderna mRNA Vaccines (2021) · cites this paper as [64]
The Results (Fig. 3; page not specified) show that tetranucleotides containing all three stop codons competed in a reticulocyte release-factor binding assay, and that UAGA required a higher concentration for complete competition. The paper does not establish the claimed UAA > UGA affinity ordering or show that UAA is a more efficient stop codon; it also notes contamination affecting the UAGA result. (LLM, conf=0.82)
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Research works printed but not linked: 16
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Cited by
Sorted by citations
Detailed Dissection and Critical Evaluation of the Pfizer/BioNTech and Moderna mRNA Vaccines
Xia, X. (2021) · Vaccines · doi:10.3390/vaccines9070734 · Cited by 201 · see citing works
Cameron, D. M., Thompson, J., March, P. E., & Dahlberg, A. E. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00235-8 · Cited by 99 · see citing works
- Authors
- Tate, W. P., Beaudet, A. L., & Caskey, C. T.
- Affiliations
- Baylor College of Medicine (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1973-08
- Volume
- 70
- Issue
- 8
- Pages
- 2350-2355
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC433733
- OpenAlex
- W2030355192
- Cited by
- 42
- References
- 0
- Citations by year
- 2021: 1 · 2016: 1
- FWCI
- 2.33
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- guanine nucleotides, GTP, elongation factors, elongation factor 2, elongation factor G, GTPase activity, fusidic acid, ribosome binding, Escherichia coli
- MeSH terms
- Animals, Base Sequence, Formates, Fusidic Acid, Genetic Code, Guanine Nucleotides, Hydrolysis, Methionine, Peptide Chain Termination, Translational, Peptide Elongation Factors, Peptide Termination Factors, Rabbits, Reticulocytes, Ribosomes, RNA, Transfer, Tritium
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