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Volume 271, Number 47, Issue of November 22, 1996 pp. 30089-30095
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Modulation of JunD·AP-1 DNA Binding Activity by AP-1-associated Factor 1 (AF-1)

(Received for publication, May 29, 1996, and in revised form, September 10, 1996)

From the Laboratory of Pathology, NCI, National Institutes of Health, Bethesda, Maryland 20892

AP-1-associated factor 1 (AF-1), is a novel protein complex that dramatically enhances the assembly of JunD-containing dimers onto AP-1 consensus sites. We describe the partial purification of AF-1 from nuclear extracts of the T-cell line MLA 144 by ionic, hydrophobic and gel filtration chromatography. AF-1 is a DNA-binding protein composed of low molecular mass polypeptides of 7-17 kDa that exists in solution as a 34-kDa complex. JunD interactions with DNA are accelerated in the presence of AF-1 through the formation of a true tri-molecular complex with JunD dimers and DNA that assembles much more rapidly on DNA than JunD alone. DNA binding analysis of AF-1 interaction with JunD·AP-1 and DNA shows that AF-1 increases the DNA binding affinity of JunD for AP-1 sites over 100-fold. DNA cleavage footprint analysis of isolated AF-1·JunD DNA complexes shows that the ternary complex makes nearly twice as many contacts with DNA than JunD dimers alone. AF-1 interacts readily, but differentially with Jun homodimers and Jun·Fos heterodimers. These findings distinguish AF-1 as a significant protein-specific modulator of AP-1·JunD in T-cells.

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