Interaction of cellular proteins with the human T-cell leukemia virus type I transcriptional control region. Purification of cellular proteins that bind the 21-base pair repeat elements.

Nuclear extracts of cultured human cells contain multiple proteins that recognize specific sequence elements within the transcriptional control region of the human retrovirus, human T-cell leukemia virus type I (HTLV-I). Here we report the purification of host expression factor 1T (HEF-1T), a DNA-binding protein from human T-lymphocytes that binds to each of the three 21-base pair repeat enhancer elements in the proviral long terminal repeats of HTLV-I and the related virus, HTLV-II. HEF-1T is composed of two polypeptides of 41 and 59 kDa. We show that HEF-1T is distinct from a second protein, present in non-lymphoid cells, that binds to overlapping sites in and near the 21-base pair repeats. This second protein is composed of a single 47-kDa polypeptide and appears to be identical to the previously described transcription factor AP-2. A third protein, also distinct from HEF-1T, binds within the first repeat. The present results suggest that there may be multiple modes of HTLV-I promoter recognition involving distinct sets of cellular proteins.