Cross-linking of tRNA at two different sites of the elongation factor Tu

Recently, we reported on the induction by kirromycin of two tRNA binding sites on elongation factor Tu. To obtain independent information on the existence of these two sites and to characterize them further, 3' oxidized tRNA was cross-linked to elongation factor Tu by [3H]borohydride reduction....

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1984-07, Vol.81 (13), p.3969-3972
Main Authors: Van Noort, J M, Kraal, B, Bosch, L, La Cour, T F, Nyborg, J, Clark, B F
Format: Article
Language:English
Subjects:
Anti-Bacterial Agents - pharmacology
Borohydrides
Escherichia coli - metabolism
Guanosine Diphosphate - metabolism
Kinetics
Macromolecular Substances
Oxidation-Reduction
Peptide Elongation Factor Tu
Peptide Elongation Factors - metabolism
Peptide Fragments - analysis
Protein Binding
Protein Conformation
Pyridones - pharmacology
RNA, Transfer - metabolism
Tritium
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Summary:Recently, we reported on the induction by kirromycin of two tRNA binding sites on elongation factor Tu. To obtain independent information on the existence of these two sites and to characterize them further, 3' oxidized tRNA was cross-linked to elongation factor Tu by [3H]borohydride reduction. Specific cross-linking occurred exclusively in the presence of kirromycin. In the case of elongation factor Tu X GDP X kirromycin, cross-linking was found at lysine-208; in elongation factor Tu X GTP X kirromycin, cross-linking was at lysine-208 and lysine-237. In both elongation factor Tu complexes, kirromycin itself was found cross-linked to lysine-357. The tRNA cross-linking sites are in agreement with the idea of two different binding sites of tRNA on elongation factor Tu.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.81.13.3969