Autophosphorylation of archaeal Cdc6 homologues is regulated by DNA
Autophosphorylation of archaeal Cdc6 homologues is regulated by DNA
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DOI：
10.1128/jb.183.18.5459-5464.2001
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发表时间：
2001-09-01
影响因子：
3.2
通讯作者：
Kelman, Z
中科院分区：
文献类型：
--
作者：
Grabowski, B;Kelman, Z
起始蛋白Cdc6（在裂殖酵母中为Cdc18）在真核生物DNA复制的起始中起重要作用。在酵母中，该蛋白质在DNA复制开始之前表达，并且被认为是将解旋酶装载到起始DNA上所必需的。然而，这种蛋白质的生物化学性质在很大程度上是未知的。使用Cdc6的三个古细菌同源物，发现蛋白质在Ser残基上自磷酸化。Cdc6的C末端的翼状螺旋结构域与DNA相互作用，其明显地调节自磷酸化反应。酵母Cdc18也被发现自磷酸化，这表明Cdc6的这种功能可能在复制起始中发挥广泛保守和重要的作用。
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.