The TFIIIB-assembling subunit of yeast transcription factor TFIIIC has both tetratricopeptide repeats and basic helix-loop-helix motifs

Abstract

The multisubunit yeast transcription factor IIIC (TFIIIC; also called τ) can undergo considerable conformational changes upon binding to the A and B blocks of tRNA genes. After binding to DNA encoding tRNA (tDNA), TFIIIC acts as an assembly factor to recruit an initiation factor, TFIIIB, via its τ131 subunit. We have cloned the gene encoding the τ131 subunit and named it TFC4. This gene is unique, essential for cell viability, and encodes a Mr 120,153 protein. Epitope-tagging and mobility-shift assays indicated the presence of a single τ131 subunit in TFIIIC-tDNA complexes. τ131 contains two sequence motifs, accounting for nearly one-half of the protein mass, that may provide a molecular explanation for the properties of TFIIIC-tDNA complex. A series of 11 copies of the tetratricopeptide repeat motif may account for the flexibility and interaction properties of TFIIIC. A motif akin to the basic helix-loop-helix motif of MyoD suggests the direct involvement of τ131 in promoting DNA binding of TFIIIB.