title: Unique modifications of translation elongation factors.
abstract: Covalent modifications of proteins often modulate their biological functions or change their subcellular location. Among the many known protein modifications, three are exceptional in that they only occur on single proteins: ethanolamine phosphoglycerol, diphthamide and hypusine. Remarkably, the corresponding proteins carrying these modifications, elongation factor 1A, elongation factor 2 and initiation factor 5A, are all involved in elongation steps of translation. For diphthamide and, in part, hypusine, functional essentiality has been demonstrated, whereas no functional role has been reported so far for ethanolamine phosphoglycerol. We review the biosynthesis, attachment and physiological roles of these unique protein modifications and discuss common and separate features of the target proteins, which represent essential proteins in all organisms.
authors.affiliation: Institute for Biochemistry and Molecular Medicine, University of Berne, Berne, Switzerland.
authors.forename: Eva
authors.initials: E
authors.lastname: Greganova
authors.forename: Michael
authors.initials: M
authors.lastname: Altmann
authors.forename: Peter
authors.initials: P
authors.lastname: Bütikofer
mesh_terms: D000818:Animals; D040061:Eukaryotic Initiation Factor-5 / Q000378:metabolism*; D006639:Histidine / Q000031:analogs & derivatives* / Q000378:metabolism; D006801:Humans; D008239:Lysine / Q000031:analogs & derivatives* / Q000378:metabolism; D020648:Peptide Elongation Factor 1 / Q000378:metabolism*; D020652:Peptide Elongation Factor 2 / Q000378:metabolism*; D010714:Phosphatidylethanolamines / Q000378:metabolism*; D011499:Protein Processing, Post-Translational
chemical_list: D040061:Eukaryotic Initiation Factor-5; D020648:Peptide Elongation Factor 1; D020652:Peptide Elongation Factor 2; D010714:Phosphatidylethanolamines; C100028:hypusine; D006639:Histidine; C027527:diphthamide; D008239:Lysine