Davydova E K, Sitikov A S, Ovchinnikov L P
FEBS Lett. 1984 Oct 29;176(2):401-5. doi: 10.1016/0014-5793(84)81206-5.
A single protein, Mr approximately 50000, is shown to be phosphorylated during incubation of a mono- and polyribosome fraction of rabbit reticulocytes with [gamma-32P]ATP at a low ionic strength. This protein has been identified as the elongation factor 1 alpha (EF-1 alpha). The phosphorylated EF-1 alpha, in contrast to the unmodified factor, is not detected in complexes with mono- and polyribosomes. It is suggested that the phosphorylation of EF-1 alpha can result in its decompartmentation from polyribosomes and thus affect the rate of protein synthesis.
在低离子强度下,用[γ-32P]ATP孵育兔网织红细胞的单核糖体和多核糖体组分时,发现一种分子量约为50000的单一蛋白质发生了磷酸化。这种蛋白质已被鉴定为延伸因子1α(EF-1α)。与未修饰的因子相比,磷酸化的EF-1α在与单核糖体和多核糖体形成的复合物中未被检测到。有人认为,EF-1α的磷酸化可能导致其从多核糖体中解离,从而影响蛋白质合成的速率。