The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Hydrolysis of Guanosine 5'-Triphosphate Associated with Binding of Aminoacyl Transfer Ribonucleic Acid to Ribosomes
Open accessAbstract
Abstract The binding of aminoacyl transfer RNA to ribosomes is a multistep reaction that is dependent on GTP and on the supernatant fraction called T. An intermediate T-GTP-aminoacyl-tRNA complex can be isolated with the GTP intact. In the work described here, the isolated complex was allowed to interact with ribosomes previously charged with polyuridylic acid and N-acetylphenylalanyl-tRNA; the phenylalanyl-tRNA moiety of the complex bound to the ribosomes, and the GTP was split into GDP and Pi. The same reaction was observed as a GTPase stimulated by T factor, aminoacyl-tRNA, message, and ribosome. This GTPase was not inhibited by sparsomycin, which blocks dipeptide formation, nor by fusidic acid, which blocks the ribosome-dependent GTPase of G factor (the supernatant factor required in addition to the T factor in the polypeptide chain elongation process). The GTPase was not affected by chlortetracycline under conditions in which the binding of aminoacyl-tRNA to the ribosomes was blocked. The 50 S ribosomal subunit alone supported the GTP hydrolysis. Both binding and GTPase paralleled each other under limiting GTP concentrations, were poorly inhibited by GDP and guanylyl 5'-methylene diphosphonate, and paralleled each other in NH4+ and Mg++ requirements and sensitivity to a sulfhydryl inhibitor. It is concluded that, although GTP hydrolysis resulted from the binding of aminoacyl-tRNA to ribosomes in a 1:1 stoichiometry, the two reactions were not tightly coupled under all experimental conditions. An improved procedure for the purification of the T and G factors is described.
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“It appears likely, however, that the initial binding of a ternary complex of EF-Tu with tRNA to the A site and the process of decoding are not affected since ribosome-dependent GTP hydrolysis by EF-Tu is unaffected by tetracycline (Gordon 1969”
From The Structural Basis for the Action of the Antibiotics Tetracycline, Pactamycin, and Hygromycin B on the 30S Ribosomal Subunit (2000) · cites this paper as Gordon 1969
In the citing paper
“More precisely, they inhibit accommodation of aminoacyl-tRNA (aa-tRNA) into the ribosomal A site (Fig. 1, reactions a and b) and, therefore, prevent the addition of new amino acids to the growing polypeptide (22, 25, 29, 48).”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [22]
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Metadata
- Authors
- Gordon, J.
- Affiliations
- Rockefeller University (US)
- Corresponding author
- Gordon, Julian
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1969-10
- Volume
- 244
- Issue
- 20
- Pages
- 5680-5686
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1565208369
- Cited by
- 146
- References
- 33
- Citations by year
- 2026: 1 · 2021: 1 · 2018: 1 · 2017: 1 · 2014: 1
- FWCI
- 11.17
- 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 › Immunology and Microbiology › Immunology › Toxin Mechanisms and Immunotoxins
- Keywords
- GTP hydrolysis, aminoacyl-tRNA binding, ribosome, T factor, general intelligence, ribosome-associated GTPase, translation elongation, 50S ribosomal subunit, polyuridylic acid, sparsomycin, fusidic acid, chlortetracycline
- MeSH terms
- Quaternary Ammonium Compounds, Bacterial Proteins, Binding Sites, Carbon Isotopes, Chemistry, Chlortetracycline, Chromatography, Chromatography, DEAE-Cellulose, Escherichia coli, Fusidic Acid, Glycols, Guanine Nucleotides, Hydroxyapatites, Ligases, Magnesium, Methods, Phenylalanine, Phosphoric Monoester Hydrolases, Phosphorus Isotopes, Polynucleotides, Ribosomes, RNA, Bacterial, RNA, Transfer, Solubility, Uracil Nucleotides, Chemical Phenomena
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
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