古细菌Cdc6同源物的自磷酸化受DNA调控。
Autophosphorylation of archaeal Cdc6 homologues is regulated by DNA.
作者信息
Grabowski B, Kelman Z
机构信息
Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850, USA.
出版信息
J Bacteriol. 2001 Sep;183(18):5459-64. doi: 10.1128/JB.183.18.5459-5464.2001.
Abstract
The initiator protein Cdc6 (Cdc18 in fission yeast) plays an essential role in the initiation of eukaryotic DNA replication. In yeast the protein is expressed before initiation of DNA replication and is thought to be essential for loading of the helicase onto origin DNA. The biochemical properties of the protein, however, are largely unknown. Using three archaeal homologues of Cdc6, it was found that the proteins are autophosphorylated on Ser residues. The winged-helix domain at the C terminus of Cdc6 interacts with DNA, which apparently regulates the autophosphorylation reaction. Yeast Cdc18 was also found to autophosphorylate, suggesting that this function of Cdc6 may play a widely conserved and essential role in replication initiation.
摘要
起始蛋白Cdc6（裂殖酵母中的Cdc18）在真核生物DNA复制起始过程中起着至关重要的作用。在酵母中，该蛋白在DNA复制起始前表达，被认为对于将解旋酶加载到起始DNA上至关重要。然而，该蛋白的生化特性在很大程度上尚不清楚。利用Cdc6的三种古细菌同源物，发现这些蛋白在丝氨酸残基上发生自磷酸化。Cdc6 C末端的翼状螺旋结构域与DNA相互作用，这显然调节了自磷酸化反应。还发现酵母Cdc18也会自磷酸化，这表明Cdc6的这种功能可能在复制起始过程中发挥广泛保守且至关重要的作用。
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