PMID: 6989608Apr 1, 1980Paper

Tyrosine residues in the C-terminal domain of the elongation factor G are essential for its interaction with the ribosome

European Journal of Biochemistry
Y B AlakhovI A Kashparov

Abstract

Chemical modification of the elongation factor G (EF-G) with tetranitromethane and iodine has been studied. It has been shown by spectrophotometric titration that EF-G contains two exposed tyrosine residues, one of which has an unusually low pK value for a phenol hydroxyl group at pH 8.5. Modification of one tyrosine residue with either tetranitromethane or iodine results in a 70--80% loss of EF-G activity in all ribosome-dependent reactions. Modification of three or four residues inhibits 90--100% of activity. Binding of EF-G with the 70-S ribosome and 50-S subunit is equally effective for protection of tyrosine residues against modification. The rate of EF-G modification with tetranitromethane is considerably higher in the presence of guanyl nucleotides than for free EF-G. The modified residues are located in the C-terminal domain of EF-G and are presumably contained in one of the sites of EF-G interaction with the ribosome.

References

Jan 15, 1978·FEBS Letters·A S GirshovichY A Ovchinnikov
Sep 1, 1979·European Journal of Biochemistry·Y B AlakhovS Y Venyaminov
Sep 26, 1966·Archives of Biochemistry and Biophysics·Y Nishizuka, F Lipmann
Jan 1, 1969·Cold Spring Harbor Symposia on Quantitative Biology·Y KaziroM Kawakita
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Citations

Jan 1, 1982·Progress in Biophysics and Molecular Biology·A Liljas
Apr 25, 2007·Advances in Genetics·Kathleen L Triman

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