STRUCTURE OF COMPLEX BETWEEN TFIIIA &ITS 31 BP DNA SITE

Stanford University, Stanford CA

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Abstract

Multiple zinc finger motifs were originally discovered in Xenopus transcription factor IIIA (TFIIIA). Each motif is an independently folded protein domain. Nine tandem zinc fingers are present in TFIIIA, allowing the protein to bind to an extensive region of the 5S RNA gene promoter. There is a relatively "standard" docking of most of the fingers represented in set into the major groove of DNA, but the GLI structure shows one finger with essentially no DNA contacts. Thus, proteins with more than 3 fingers may have highly divergent docking modes. The goal of the present study is to examine a still longer complex.