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Vol. 10, Issue 3, 567-580, March 1999

OBA/Ku86: DNA Binding Specificity and Involvement in Mammalian DNA Replication

Marcia T. Ruiz,* Diamanto Matheos,*dagger Gerald B. Price,* and Maria Zannis-Hadjopoulos*dagger Dagger

 *McGill Cancer Centre and  dagger Department of Biochemistry, McGill University, Montreal, Quebec, Canada

Ors-binding activity (OBA) was previously semipurified from HeLa cells through its ability to interact specifically with the 186-basepair (bp) minimal replication origin of ors8 and support ors8 replication in vitro. Here, through competition band-shift analyses, using as competitors various subfragments of the 186-bp minimal ori, we identified an internal region of 59 bp that competed for OBA binding as efficiently as the full 186-bp fragment. The 59-bp fragment has homology to a 36-bp sequence (A3/4) generated by comparing various mammalian replication origins, including the ors. A3/4 is, by itself, capable of competing most efficiently for OBA binding to the 186-bp fragment. Band-shift elution of the A3/4-OBA complex, followed by Southwestern analysis using the A3/4 sequence as probe, revealed a major band of ~92 kDa involved in the DNA binding activity of OBA. Microsequencing analysis revealed that the 92-kDa polypeptide is identical to the 86-kDa subunit of human Ku antigen. The affinity-purified OBA fraction obtained using an A3/4 affinity column also contained the 70-kDa subunit of Ku and the DNA-dependent protein kinase catalytic subunit. In vitro DNA replication experiments in the presence of A3/4 oligonucleotide or anti-Ku70 and anti-Ku86 antibodies implicate Ku in mammalian DNA replication.

Dagger    Corresponding author. E-mail address: hadjopoulos{at}medcor.mcgill.ca.

Molecular Biology of the Cell
Vol. 10, 567-580, March 1999
Copyright © 1999 by The American Society for Cell Biology


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