Autophosphorylation of archaeal Cdc6 homologues is regulated by DNA

被引：41

作者：

Grabowski, B ^{[1
]}

Kelman, Z ^{[1
]}

机构：

[1] Univ Maryland, Maryland Biotechnol Inst, Ctr Adv Res Biotechnol, Rockville, MD 20850 USA

来源：

JOURNAL OF BACTERIOLOGY | 2001年 / 183卷 / 18期

关键词：

D O I：

10.1128/JB.183.18.5459-5464.2001

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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.

引用

页码：5459 / 5464

页数：6

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