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Nucleic Acids Research, 1989, Vol. 17, No. 11 4061-4075
© 1989

MOLECULAR BIOLOGY

Mutant analysis of protein interactions with a nuclear factor I binding site in the SL3-3 virus enhancer

Pia Nilsson, Bengt Hallberg, Anders Thomell and Thomas Grundstrom

Department of Applied Cell and Molecular Biology, University of Umea S-901 87 Umeiå, Sweden

Received March 2, 1989. Revised May 11, 1989. Accepted May 11, 1989.

Nuclear factor I (NFI) is shown to be of importance for the activity of the enhancer element of a T-cell leukemogenic murine retrovirus, SL3-3, and for the regulation of this element by glucocorticoid. Each nucleotide of the binding site of the NFI proteins was mutated, and the effects of the mutations were quantitated with an electrophoretic mobility shift assay. Mutations in the inverted repeat of the binding site have symmetric effects which strongly support the notion that NFI proteins preferentially bind to dyad symmetry sites. Such binding sites were shown to be more than 100 fold stronger than the corresponding single binding sites. We find dyad symmetry sequences which are much stronger NFI binding sites than NFI sites identified in different genes and also stronger than previously proposed consensus binding sequences for NFI.


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