Characterization of reticulocyte release factor
Open accessAbstract
The release factor (RF) of reticulocytes has been purified to greater than 75% homogeneity. The RF has a native molecular weight of 105,000 and subunit molecular weight of 56,500. The RF protein will bind to reticulocyte ribosomes in response to UAAA, UAGA, or UGAA and therefore participates in codon recognition. The fraction possess a ribosome-dependent GTPase activity. The RF is stimulated in its activity by a second protein fraction.
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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 [63]
UAA (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 [63]
The translation termination signal is more than a stop codon, including the downstream +4 site (tetranucleotide stop signal).
“It has long been recognized that the translation termination signal is more than a stop codon [86,87], leading to an early proposal of tetranucleotide stop signal including the downstream +4 site [63,65,87,88].”
From Detailed Dissection and Critical Evaluation of the Pfizer/BioNTech and Moderna mRNA Vaccines (2021) · cites this paper as [63]
The 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 [63]
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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
- Authors
- Konecki, D. S., Aune, K. C., Tate, W., & Caskey, C. T.
- Affiliations
- Texas Medical Center (US)
- ORCID
- Tate, W
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1977-07
- Volume
- 252
- Issue
- 13
- Pages
- 4514-4520
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2101908148
- Cited by
- 110
- References
- 0
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2023: 2 · 2022: 1 · 2021: 2 · 2019: 1 · 2018: 2 · 2017: 1 · 2016: 2 · 2015: 1 · 2014: 5 · 2013: 1 · 2012: 2
- FWCI
- 0.92
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- 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 › Molecular Biology › RNA Research and Splicing
- Keywords
- release factors, reticulocytes, protein purification, molecular weight, ribosome binding, codon recognition, UAA codon, UAG codon, UGA codon, translation termination
- MeSH terms
- Animals, Blood Protein Electrophoresis, Blood Proteins, Centrifugation, Density Gradient, Chemistry, Chromatography, Gel, Electrophoresis, Polyacrylamide Gel, Guanosine Triphosphate, Hydrolysis, Molecular Weight, Peptide Termination Factors, Rabbits, Reticulocytes, Ribosomes, Chemical Phenomena, In Vitro Techniques
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