| Autor: |
Price, Nigel T., Redpath, Nicholas T., Severinov, Konstantin V., Campbell, David G., Russell, J.M., Proud, Christopher G. |
| Zdroj: |
FEBS Letters; May 1991, Vol. 282 Issue: 2 p253-258, 6p |
| Abstrakt: |
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. |
| Databáze: |
Supplemental Index |
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