An element of symmetry in yeast TATA-box binding protein transcription factor IID. Consequence of an ancestral duplication?
TATA-box binding factor TFIID is one of the key factors in transcriptional activation. Surprisingly, the yeast TFDII protein [(1989) Nature 341, 299-303; (1989) Cell 56, 1173-1181; (1989) Proc. Natl. Acad. Sci USA 86, 7785-7789] reveals only limited homology with other DNA-binding proteins. From computer-assisted searches we infer that yeast TFIID possesses a domain structure in which homologous segments are repeated. The greatest similarity is found between two segments, each 33 amino acids in length, in which the positions of four basic residues are strictly conserved. The high homology is also reflected at the gene level. Implications of this novel type of domain structure for possible interactions in transcriptional activation are discussed.
Stucka
R
R
Institut für Physiologische Chemie, Universität München, FRG.
Feldmann
H
H
D000595:Amino Acid Sequence; D001483:Base Sequence; D008954:Models, Biological; D008969:Molecular Sequence Data; D015394:Molecular Structure; D005810:Multigene Family; D012441:Saccharomyces cerevisiae / Q000032:analysis / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid; D035362:Transcription Factor TFIID; D014157:Transcription Factors / Q000235:genetics*
D035362:Transcription Factor TFIID; D014157:Transcription Factors