FEBS Letters | |
Mechanism of elongation factor 2 (EF‐2) inactivation upon phosphorylation Phosphorylated EF‐2 is unable to catalyze translocation | |
Davydova, Elena K.1  Ryazanov, Alexey G.1  | |
[1] Institute of Protein Research, Academy of Sciences of the USSR, 142292 Pushchino, Moscow Region, USSR | |
关键词: Elongation factor 2; Protein phosphorylation; EF-2 kinase; Calmodulin; Ribosomal translocation; Translational control; EF-1; elongation factor 1; EF-2; elongation factor 2; GMPPCP; guanosine 5′-(β; γ-methylene)triphosphate; GMPPNP; guanosine 5′-(β; γ-imino)triphosphate; | |
DOI : 10.1016/0014-5793(89)81452-8 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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.
【 授权许可】
Unknown
【 预 览 】
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RO201912020292292ZK.pdf | 311KB | download |