Selective photooxidation of histidine residues in polypeptide chain elongation factor Tu from E. coli

Journal of Biochemistry
S Nakamura, Y Kaziro

Abstract

When EF-Tu was photooxidized for 20 min at 0 degrees C in the presence of 10 microM GDP and 5 microM rose bengal, the activity to promote the binding of [14C]Phe-tRNA to ribosomes was rapidly lost, while the activity to bind [3H]GDP remained intact. The activity of EF-Tu to interact with Phe-tRNA and ribosomes, as assessed by protection of [14C]Phe-tRNA against RNase A digestion and by methanol-induced uncoupled GTPase activity, respectively, was also inactivated under the above conditions. It was found, however, that these activities were fully protected in the presence of aminoacyl-tRNA and GTP, indicating that the active site(s) of EF-Tu for interaction with aminoacyl-tRNA and ribosomes could be protected against photooxidation in the ternary aminoacyl-tRNA . EF-Tu . GTP complex. Comparison of the amino acid composition of EF-Tu photooxidized in the form of EF-Tu . GDP with that of the intact EF-Tu revealed that only 1.4 residues of histidine were damaged. On the other hand, no histidine residue was lost when EF-Tu was oxidized in the presence of both aminoacyl-tRNA and GTP. The photooxidized EF-Tu . GDP was then partially degraded with trypsin and each of the resulting tryptic fragments, D, B, and C (Arai, Nakamura, Arai, K...Continue Reading

Citations

Jun 15, 1984·European Journal of Biochemistry·B Antonsson, R Leberman
Jan 21, 2016·The Journal of Biological Chemistry·Rayakorn YutthanasirikulYoshitaka Nishiyama
Jan 28, 1987·Biochimica Et Biophysica Acta·J Jonák, I Rychlík
Jan 2, 2007·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·J Jonák

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