α-晶体蛋白的自身激酶活性在体外抑制其与小鼠γD/E/F-晶体蛋白启动子中DOTIS元件的特异性相互作用。
Autokinase activity of alpha-crystallin inhibits its specific interaction with the DOTIS element in the murine gamma D/E/F-crystallin promoter in vitro.
作者信息
Pietrowski D, Graw J
机构信息
GSF-National Research Center for Environment and Health, Institute of Mammalian Genetics, Neuherberg, Germany.
出版信息
Biol Chem. 1997 Oct;378(10):1183-6.
In a previous report we demonstrated the in vitro interaction of alpha-crystallin with an element downstream of the transcriptional initiation site (DOTIS) of the murine gamma E-crystallin promoter (Pietrowski et al., 1994, Gene 144, 171-178). The aim of the present study was to investigate the influence of phosphorylation on this particular interaction. We could demonstrate that the autophosphorylation of alpha-crystallin leads to a complete loss of interaction with the DOTIS element, however, PKA-dependent phosphorylation of alpha-crystallin is without effect on the interaction. It is hypothesized that the autophosphorylation of alpha-crystallin might be involved in regulatory mechanisms of the murine gamma D/E/F-crystallin gene expression.
在之前的一份报告中，我们展示了α-晶状体蛋白与小鼠γE-晶状体蛋白启动子转录起始位点下游元件（DOTIS）的体外相互作用（Pietrowski等人，1994年，《基因》144卷，171 - 178页）。本研究的目的是探究磷酸化对这种特定相互作用的影响。我们能够证明，α-晶状体蛋白的自磷酸化导致其与DOTIS元件的相互作用完全丧失，然而，α-晶状体蛋白的蛋白激酶A（PKA）依赖性磷酸化对该相互作用没有影响。据推测，α-晶状体蛋白的自磷酸化可能参与了小鼠γD/E/F-晶状体蛋白基因表达的调控机制。
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