Location of seven post-translational modifications in rabbit elongation factor 1α including dimethyllysine, trimethyllysine, and glycerylphosphorylethanolamine

T. E. Dever, C. E. Costello, C. L. Owens, T. L. Rosenberry, W. C. Merrick

Research output: Contribution to journalArticle

85 Scopus citations

Abstract

Amino acid sequencing of a large number of chemical and enzymatic cleavage products of elongation factor 1α purified from rabbit reticulocyte has identified seven post-translationally modified residues. Five of the modifications are methylations of lysine residues yielding dimethyllysine at residues 55 and 165 and trimethyllysine at residues 36, 79, and 318. The two remaining post-translational modifications involve the addition of ethanolamine to glutamic acid residues 301 and 374, as reported previously (Rosenberry, T.L., Krall, J.A., Dever, T.E., Haas, R., Louvard, D., and Merrick, W.C. (1989) J. Biol. Chem. 264, 7096-7099). Fast atom bombardment mass spectrometry and fast atom bombardment tandem mass spectrometry have been used to analyze peptides containing these modified residues. The analyses have determined that glycerylphosphorylethanolamine has been attached to the glutamic acid residues. An analysis of the amino acid sequence surrounding each of the three types of modification has indicated no similarities. Therefore, it ssems likely that the modifying enzymes do not recognize a specific amino acid sequence but rather the three-dimensional presentation of either amino or carboxyl residues in the elongation factor 1α structure.

Original languageEnglish (US)
Pages (from-to)20518-20525
Number of pages8
JournalJournal of Biological Chemistry
Volume264
Issue number34
StatePublished - Dec 20 1989

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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