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Nucleic Acids Research, 1989, Vol. 17, No. 19 7761-7770
© 1989

MOLECULAR BIOLOGY

A DNA-binding domain or human transcription factor IIIC2

Pierre A. Boulanger+, Noelle D. L'Etoile and Arnold J. Berk*

Molecular Biology Institute and Department of Microbiology, University of California Los Angeles, CA 90024–1570, USA

+Present address: Laboratoire de Virologie et Pathogenese Moleculaires, Institut de Biologie, Faculté de Medecine, 34060 Montpellier, France

*To whom correspondence should be addressed

Received June 26, 1989. Revised August 25, 1989. Accepted August 25, 1989.

Transcription factor IIIC2 is required for in vitro transcription of the adenovirus 2 VA1 gene and binds with high affinity to its B-box promoter element which is an 18 bp perfect inverted repeat. Partial proteolysis of TFIIIC2 with chymotrypsin and Staphylococcus aureus V8 protease yielded a species which produced a discrete band in a gel shift assay with about twice the mobility of the undigested complex. Chymotrypsin-digested TFIIIC2 produced a DNase I footprint virtually identical to that of the undigested protein, but the stability of the protein-VA1 DNA complex was drastically reduced and the in vitro transcriptional activity was eliminated. These results indicate that a chymotrypsin-resistant domain of TFIIIC2 binds to the B-box sequence. We speculate that stable binding requires protease sensitive cooperative interactions between TFIIIC2 DNA-binding domains.


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