Nucleic Acids Research, 1988, Vol. 16, No. 10 4419-4435
© 1988
Articles |
A quantitative analysis of nuclear factor I/DNA interactions
Institut f
r Biochemie, Universität Mnchen Karlstrasse 23, D-8000 Mnchen 2, FRG
Received February 12, 1988. Revised April 12, 1988. Accepted April 12, 1988.
Nuclear factor I (NFI) was purified to homogeneity from porcine liver by DNA-affinity chromatography and displays a single band with a molecular weight of 36 kDa in SDS-polyacrylamide gels. The purified protein was used to determine absolute equilibrium binding constants by gel retardation techniques for a variety of DNA fragments with genuine or mutated NFI binding sites and a number of DNA fragments derived from various eukaryotic promoters carrying the CCAAT-box as a half-site for NFI binding. We present a model which allows prediction of the functional significance of mutated NFI binding-sites from sequence data. The data suggest that the single molecular species of NFI from porcine liver may not be able to recognize and activate the -CCAAT- promoter element in vivo without additional interactions, e.g. with other proteins.
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