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The upstream stimulatory factor 1 (USF1) belongs to the basic helix-loop-helix leucine zipper (b/HLH/Z) transcription factor family, recognizing the CACGTG DNA motive as a dimer and playing an important role in the regulation of transcription in a variety of cellular and viral promoters. In this study we investigate the USF1 b/HLH/Z domain and its complexes with DNA by small angle x-ray scattering. We present low resolution structural models of monomeric b/HLH/Z USF1 in the absence of DNA and USF1 dimeric (b/HLH/Z)2-DNA and tetrameric (b/HLH/Z)4-DNA2 complexes. The data reveal a concentration-dependent USF1 dimer (b/HLH/Z)2-DNA-tetramer (b/HLH/Z)4-DNA2 equilibrium. The ability of b/HLH/Z USF1 to form a tetrameric assembly on two distant DNA binding sites as a consequence of increased protein concentration suggest a USF1 concentration-dependant mechanism of transcription activation involving DNA loop formation.