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
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