Peter Weil
Faculty Member
Last active: 11/4/2015

Analysis of structure-function relationships of yeast TATA box binding factor TFIID.

Horikoshi M, Yamamoto T, Ohkuma Y, Weil PA, Roeder RG
Cell. 1990 61 (7): 1171-8

PMID: 2194665 · DOI:10.1016/0092-8674(90)90681-4

A systematic series of N-terminal, C-terminal, and internal deletion mutants of S. cerevisiae TFIID were expressed in vitro and tested for TATA box binding and basal level transcription activities using, respectively, DNA mobility shift and in vitro transcription assays. The domains responsible for these activities were colocalized to a surprisingly large region containing C-terminal residues 63-240. This region was noted previously to contain potentially interesting structural motifs (central basic core, direct repeats, and sigma factor homology) and, more recently, to be highly conserved among TFIID from different species. Deletion mutant cotranslation studies revealed that TFIID binds DNA as a monomer. The implications of these results for TFIID structure and function are discussed.

MeSH Terms (14)

Base Sequence Chromosome Deletion Molecular Sequence Data Mutation Oligonucleotide Probes Plasmids Promoter Regions, Genetic Protein Binding Protein Biosynthesis Restriction Mapping Saccharomyces cerevisiae Transcription, Genetic Transcription Factors Transcription Factor TFIID

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