A bipartite DNA binding domain composed of direct repeats in the TATA box binding factor TFIID.

Yamamoto T, Horikoshi M, Wang J, Hasegawa S, Weil PA, Roeder RG
Proc Natl Acad Sci U S A. 1992 89 (7): 2844-8

PMID: 1557391 · PMCID: PMC48759 · DOI:10.1073/pnas.89.7.2844

Point mutations in residues comprising the interrupted direct repeats of TFIID eliminated DNA binding in an electrophoretic mobility shift assay. In contrast, mutations in nonconserved residues within the direct repeat regions or in lysine residues comprising the intervening basic repeat had no effect on DNA binding. However, small spacing changes (addition or deletion of one to three residues) in the basic repeat eliminated DNA binding. These results argue for a bipartite DNA binding domain composed of direct repeats with a strict spacing and orientation. Surprisingly, some direct repeat mutations that inhibited DNA binding failed to show a corresponding inhibition of basal transcription, indicating compensating interactions of TFIID with other general factors. The implications of these and other recent results for TFIID structure, promoter recognition, and interactions with other factors are discussed.

MeSH Terms (14)

Amino Acid Sequence Binding Sites DNA-Binding Proteins Fungal Proteins Molecular Sequence Data Mutagenesis, Site-Directed Promoter Regions, Genetic Regulatory Sequences, Nucleic Acid Saccharomyces cerevisiae Structure-Activity Relationship TATA Box Transcription, Genetic Transcription Factors Transcription Factor TFIID

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