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PMID: 9447997 Published · ppublish English Journal Article

The yeast TAF145 inhibitory domain and TFIIA competitively bind to TATA-binding protein.

Molecular and cellular biology ·Vol. 18 ·No. 2 ·1998-02-00 ·Pages 1003-12

Kokubo T, Swanson MJ, Nishikawa JI, Hinnebusch AG, Nakatani Y

Abstract

The Drosophila 230-kDa TFIID subunit (dTAF230) interacts with the DNA binding domain of TATA box-binding protein (TBP) which exists in the same complex. Here, we characterize the inhibitory domain in the yeast TAF145 (yTAF145), which is homologous to dTAF230. Mutation studies show that the N-terminal inhibitory region (residues 10 to 71) can be divided into two subdomains, I (residues 10 to 37) and II (residues 46 to 71). Mutations in either subdomain significantly impair function. Acidic residues in subdomain II are important for the interaction with TBP. In addition, yTAF145 interaction is impaired by mutating the basic residues on the convex surface of TBP, which are crucial for interaction with TFIIA. Consistently, TFIIA and yTAF145 bind competitively to TBP. A deletion of the inhibitory domain of yTAF145 leads to a temperature-sensitive growth phenotype. Importantly, this phenotype is suppressed by overexpression of the TFIIA subunits, indicating that the yTAF145 inhibitory domain is involved in TFIIA function.

MeSH Terms
Amino Acid Sequence Animals Binding Sites Binding, Competitive DNA-Binding Proteins/chemistry,metabolism Drosophila Fungal Proteins/chemistry,metabolism Molecular Sequence Data Osmolar Concentration Protein Binding Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins TATA-Binding Protein Associated Factors TATA-Box Binding Protein Transcription Factor TFIIA Transcription Factor TFIID Transcription Factors/chemistry,metabolism
Chemicals
DNA-Binding Proteins Fungal Proteins Saccharomyces cerevisiae Proteins TAF1 protein, S cerevisiae TATA-Binding Protein Associated Factors TATA-Box Binding Protein Transcription Factor TFIIA Transcription Factor TFIID Transcription Factors
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Kokubo T
Laboratory of Molecular Growth Regulation, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA. kokubo@bs.aist-nara.ac.jp
Swanson M J
Nishikawa J I
Hinnebusch A G
Nakatani Y
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/MCB.18.2.1003
Email
kokubo@bs.aist-nara.ac.jp
Published
1998-02-00
Pages
1003-12
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC108812
Subset
IM
External Links
PubMed source DOI: 10.1128/MCB.18.2.1003 PMC Full Text View journal details
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