Hydrolysis of Guanosine 5'-Triphosphate Associated with Binding of Aminoacyl Transfer Ribonucleic Acid to Ribosomes

Gordon, Julian

doi:10.1016/s0021-9258(18)63613-0

Cited by 146RNA and protein synthesis mechanismsRNA modifications and cancerToxin Mechanisms and Immunotoxins

Hydrolysis of Guanosine 5'-Triphosphate Associated with Binding of Aminoacyl Transfer Ribonucleic Acid to Ribosomes

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Gordon, Julian·1969·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(18)63613-0

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Abstract

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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The initial binding of a ternary complex of EF-Tu with tRNA to the A site and the process of decoding are likely not affected by tetracycline, since ribosome-dependent GTP hydrolysis by EF-Tu is unaffected by tetracycline.
“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
Typical tetracyclines inhibit accommodation of aminoacyl-tRNA into the ribosomal A site and prevent addition of new amino acids to the growing polypeptide.
“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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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)
DOI: 10.1016/s0021-9258(18)63613-0
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: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 18659 d)
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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Hydrolysis of Guanosine 5'-Triphosphate Associated with Binding of Aminoacyl Transfer Ribonucleic Acid to Ribosomes

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