Mechanism of elongation factor 2 (EF‐2) inactivation upon phosphorylation Phosphorylated EF‐2 is unable to catalyze translocation
- 17 July 1989
- journal article
- Published by Wiley in FEBS Letters
- Vol. 251 (1-2), 187-190
- https://doi.org/10.1016/0014-5793(89)81452-8
Abstract
Previously we have found that elongation factor 2 (EF-2) from mammalian cells can be phosphorylated by a special Ca2+/calmodulin-dependent protein kinase (EF-2 kinase). Phosphorylation results in complete inactivation of EF-2 in the poly(U)-directed cell-free translation system. However, the partial function of EF-2 affected by phosphorylation remained unknown. Here we show that phosphorylated EF-2, unlike non-phosphorylated EF-2, is unable to switch ribosomes carrying poly(U) and Phe-tRNA in the A site to a puromycin-reactive state. Thus, phosphorylation of EF-2 seems to block its ability to promote a shift of the aminoacyl(peptidyl)-tRNA from the A site to the P site i.e. translocation itself.This publication has 12 references indexed in Scilit:
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