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Journal of Bacteriology, September 2001, p. 5459-5464, Vol. 183, No. 18
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.18.5459-5464.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Autophosphorylation of Archaeal Cdc6 Homologues Is Regulated by DNA

Beatrice Grabowski and Zvi Kelman*

Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850

Received 30 April 2001/Accepted 19 June 2001

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.

* Corresponding author. Mailing address: CARB/UMBI, 9600 Gudelsky Dr., Rockville, MD 20850. Phone: (301) 738-6294. Fax: (301) 738-6255. E-mail: kelman{at}carb.nist.gov.

Journal of Bacteriology, September 2001, p. 5459-5464, Vol. 183, No. 18
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.18.5459-5464.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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