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Nucleic Acids Research, 1988, Vol. 16, No. 1 199-211
© 1988

Articles

Factor D is a selective single-stranded oligodeoxythymidine binding protein

M. Fry1,2,*, F.W. Perrino2, A. Levy1 and L.A. Loeb2

1The Rappaport Institute for Research in the Medical Sciences and Unit of Biochemistry, Faculty of Medicine, Technion-Israel Institute of Technology PO Box 9649, Haifa 31096, Israel 2The Joseph Gottstein Memorial Cancer Research Laboratory, Department of Pathology SM-30, University of Washington Seattle, WA 98195, USA

*To whom correspondence should be addressed

Received September 11, 1987. Revised November 20, 1987. Accepted December 1, 1987.

Factor D, a protein purified from rabbit liver that selectively enhances traversal of template oligodeoxythymidine tracts by diverse DNA polymerases, was examined for the sequence specificity of its binding to DNA. Terminally [32P]-labeled oligomers with the sequence 5'-d[AATTC(N)16G]-3', N being dT, dA, dG, or dC, were interacted with purified factor D and examined for the formation of protein-DNA complexes that exhibit retarded electrophoretic mobility under nondenaturing conditions. Whereas significant binding of factor D to 5'-d[AATTC(T)16G]-3' is detected, there is no discernable association between this protein and oligomers that contain 16 contiguous moieties of dG, dA, or dC. Furthermore, factor D does not form detectable complexes with the duplexes oligo(dA)·oligo(dT) or poly(dA)·poly(dT). The preferential interaction of factor D with single-stranded poly(dT) is confirmed by experiments in which the polymerase-enhancing activity of this protein is protected by poly(dT) against heat inactivation two- and four-fold more efficiently than by poly(dA) or poly(dA)·poly(dT), respectively.


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