FEBS Letters | |
Identification of the phosphorylation sites in elongation factor‐2 from rabbit reticulocytes | |
Russell, J.M.3  Severinov, Konstantin V.1  Redpath, Nicholas T.3  Proud, Christopher G.3  Campbell, David G.2  Price, Nigel T.3  | |
[1] Institute of Protein Research, Academy of Sciences of USSR, Pushchino, Moscow Region, USSR;MRC Protein Phospharylation Group, Department of Biochemistry, University of Dundee, DD1 4HN, UK;Department of Biochemistry, School of Medical Sciences, University of Bristol, University Walk, Bristol, BS8 1TD, UK | |
关键词: Protein synthesis; Elongation factor-2; Protein phosphorylation; Protein kinase; Calcium/calmodulin; Rabbit reticulocyte; eEF-2; eukaryotic elongation factor-2; IEF; isoelectric focusing; SDS-PAGE; sodium dodecyl sulphate-polyacrylamide gel electrophoresis; | |
DOI : 10.1016/0014-5793(91)80489-P | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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-Thr14-Asp-Thr18-Arg. The same sites are labelled in eEF-2 isolated from reticulocyte lysates.
【 授权许可】
Unknown
【 预 览 】
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