An element of symmetry in yeast TATA‐box binding protein transcription factor IID

FEBS Letters

Feldmann, Horst¹  Stucka, Rolf¹ 

[1] Institut für Physiologische Chemie der Universität München, Schillerstraße 44, D-8000 München 2, FRG

关键词: Transcription factor IID (TFIID);    Transcription factor;    TATA-box;    Transcriptional Regulation;    Domain structure;    Gene duplication;   

DOI  :  10.1016/0014-5793(90)80558-Z

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown