Oldfield S, Proud C G
Department of Biochemistry, School of Medical Sciences, University of Bristol, UK.
FEBS Lett. 1993 Jul 19;327(1):71-4. doi: 10.1016/0014-5793(93)81042-x.
In mammalian cells, protein synthesis can be regulated at the level of elongation by the phosphorylation of elongation factor 2 (eEF-2) by a highly specific Ca2+/calmodulin-dependent kinase. In this report, we show that eEF-2 from a cell line derived from the insect, Spodoptera frugiperda, is a substrate for mammalian eEF-2 kinase and that phosphorylation is Ca(2+)-dependent. Furthermore, two-dimensional peptide mapping shows that the kinase phosphorylates the same sites in Spodoptera eEF-2 as those phosphorylated in the rabbit protein. However, we were unable to detect an eEF-2 kinase in Spodoptera cells.
在哺乳动物细胞中,蛋白质合成可通过一种高度特异性的Ca2+/钙调蛋白依赖性激酶使延伸因子2(eEF-2)磷酸化,从而在延伸水平上受到调控。在本报告中,我们表明,源自昆虫草地贪夜蛾的细胞系中的eEF-2是哺乳动物eEF-2激酶的底物,且磷酸化是Ca(2+)依赖性的。此外,二维肽图显示,该激酶使草地贪夜蛾eEF-2中的相同位点发生磷酸化,就如同在兔蛋白中发生磷酸化的位点一样。然而,我们在草地贪夜蛾细胞中未能检测到eEF-2激酶。