title: Identification of the phosphorylation sites in elongation factor-2 from rabbit reticulocytes.
abstract: The sites in eukaryotic elongation factor eEF-2 phosphorylated by the Ca2+/calmodulin-dependent eEF-2 kinase in vitro have been identified. The kinase catalysed the rapid incorporation of one mol of phosphate per mol eEF-2 and the slower incorporation of a second mol. All the phosphorylation sites in eEF-2 are contained in the CNBr fragment corresponding to residues 22-155. Tryptic digestion of phosphorylated eEF-2 yielded 3 phosphopeptides, one being unique to monophosphorylated eEF-2. The phosphorylation sites were identified as threonine residues 56 and 58, the former being more rapidly phosphorylated. Ala-Gly-Glu-Thr-Phe-Thr56-Asp-Thr58-Arg. The same sites are labelled in eEF-2 isolated from reticulocyte lysates.
authors.affiliation: Department of Biochemistry, School of Medical Sciences, University of Bristol, UK.
authors.forename: N T
authors.initials: NT
authors.lastname: Price
authors.forename: N T
authors.initials: NT
authors.lastname: Redpath
authors.forename: K V
authors.initials: KV
authors.lastname: Severinov
authors.forename: D G
authors.initials: DG
authors.lastname: Campbell
authors.forename: J M
authors.initials: JM
authors.lastname: Russell
authors.forename: C G
authors.initials: CG
authors.lastname: Proud
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D007526:Isoelectric Point; D008969:Molecular Sequence Data; D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors / Q000737:chemistry / Q000378:metabolism*; D010446:Peptide Fragments / Q000737:chemistry; D010449:Peptide Mapping; D010750:Phosphoproteins / Q000737:chemistry / Q000378:metabolism; D010766:Phosphorylation; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism*; D013997:Time Factors
chemical_list: D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors; D010446:Peptide Fragments; D010750:Phosphoproteins