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

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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 - 1989
Externally publishedYes

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Peptide Elongation Factor 1
Fast Atom Bombardment Mass Spectrometry
Protein Sequence Analysis
Post Translational Protein Processing
Glutamic Acid
Rabbits
Amino Acids
Ethanolamine
Mass spectrometry
Reticulocytes
Tandem Mass Spectrometry
Methylation
Lysine
Amino Acid Sequence
Atoms
Peptides
Enzymes
glycerophosphoethanolamine
trimethyllysine

ASJC Scopus subject areas

  • Biochemistry

Cite this

Location of seven post-translational modifications in rabbit elongation factor 1α including dimethyllysine, trimethyllysine, and glycerylphosphorylethanolamine. / Dever, T. E.; Costello, C. E.; Owens, C. L.; Rosenberry, T. L.; Merrick, W. C.

In: Journal of Biological Chemistry, Vol. 264, No. 34, 1989, p. 20518-20525.

Research output: Contribution to journalArticle

Dever, T. E. ; Costello, C. E. ; Owens, C. L. ; Rosenberry, T. L. ; Merrick, W. C. / Location of seven post-translational modifications in rabbit elongation factor 1α including dimethyllysine, trimethyllysine, and glycerylphosphorylethanolamine. In: Journal of Biological Chemistry. 1989 ; Vol. 264, No. 34. pp. 20518-20525.
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T1 - Location of seven post-translational modifications in rabbit elongation factor 1α including dimethyllysine, trimethyllysine, and glycerylphosphorylethanolamine

AU - Dever, T. E.

AU - Costello, C. E.

AU - Owens, C. L.

AU - Rosenberry, T. L.

AU - Merrick, W. C.

PY - 1989

Y1 - 1989

N2 - 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.

AB - 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.

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