Identification of the phosphorylation sites in elongation factor‐2 from rabbit reticulocytes

FEBS Letters

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