Identification of Highly Conserved Amino-terminal Segments of dTAFII230 and yTAFII145 That Are Functionally Interchangeable for Inhibiting TBP-DNA Interactions in Vitro and in Promoting Yeast Cell Growth in Vivo

Autor: Tsuyoshi Miyake, Tomohiro Kotani, Masashi Kawaichi, Tetsuro Kokubo, Yoshihiro Tsukihashi, Yoshihiro Nakatani, Alan G. Hinnebusch
Rok vydání: 1998
Předmět:
Saccharomyces cerevisiae Proteins
Multiprotein complex
Genotype
Recombinant Fusion Proteins
Molecular Sequence Data
genetic processes
Mutant
Saccharomyces cerevisiae
information science
macromolecular substances
Biology
Biochemistry
Conserved sequence
Fungal Proteins
Transcription Factors
TFII
Animals
Drosophila Proteins
Humans
Amino Acid Sequence
DNA
Fungal
Molecular Biology
Peptide sequence
Conserved Sequence
Histone Acetyltransferases
chemistry.chemical_classification
TATA-Binding Protein Associated Factors
Sequence Homology
Amino Acid
Cell Biology
Alanine scanning
biology.organism_classification
Molecular biology
Amino acid
Cell biology
DNA-Binding Proteins
Phenotype
chemistry
Transcription Factor TFIID
health occupations
Insect Proteins
Drosophila
Sequence Alignment
Transcription Factors
Zdroj: Journal of Biological Chemistry. 273:32254-32264
ISSN: 0021-9258
DOI: 10.1074/jbc.273.48.32254
Popis: TFIID is a multiprotein complex composed of TBP and several TAFIIs. Small amino-terminal segments (TAF N-terminal domain (TAND)) of Drosophila TAFII230 (dTAFII230) and yeast TAFII145 (yTAFII145) bind strongly to TBP and inhibit TBP-DNA interactions. yTAFII145 TAND (yTAND) was divided into two subdomains, yTANDI10-37 and yTANDII46-71, that function cooperatively. Here, we identify dTANDII within the amino terminus of dTAFII230 at 118-143 amino acids in addition to dTANDI18-77, reported previously. dTANDII exhibits pronounced sequence similarity to yTANDII, and the two were shown to be functionally equivalent in binding to TBP and inhibiting TBP-DNA interactions in vitro. Alanine scanning mutation analysis demonstrated that Phe-57 (yTANDII) and Tyr-129 (dTANDII) are critically required for the interaction with TBP. Yeast strains containing mutant yTAFII145 lacking yTANDI or yTANDII showed a temperature-sensitive growth phenotype. The conserved core of dTANDII could substitute for the yTANDII core, and Phe-57 or Tyr-129 described above was critically required for the function of this segment in promoting normal cell growth at 37 degreesC. In these respects, the impact of yTANDII mutations on cell growth paralleled their effects on TBP binding in vitro, strongly suggesting that the yTAFII145-TBP interaction and its negative effects on TFIID binding to core promoters are physiologically important.
Databáze: OpenAIRE
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