Abstract
General transcription factor TFIID consists of TATA box-binding protein (TBP) and TBP-associated factors (TAF(II)s), which together play a central role in both positive and negative regulation of transcription. The N-terminal region of the 230 kDa Drosophila TAF(II) (dTAF(II)230) binds directly to TBP and inhibits TBP binding to the TATA box. We report here the solution structure of the complex formed by dTAF(II)230 N-terminal region (residues 11-77) and TBP. dTAF(II)230(11-77) comprises three alpha helices and a beta hairpin, forming a core that occupies the concave DNA-binding surface of TBP. The TBP-binding surface of dTAF(II)230 markedly resembles the minor groove surface of the partially unwound TATA box in the TBP-TATA complex. This protein mimicry of the TATA element surface provides the structural basis of the mechanism by which dTAF(II)230 negatively controls the TATA box-binding activity within the TFIID complex.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Crystallography, X-Ray
-
DNA-Binding Proteins / chemistry*
-
DNA-Binding Proteins / metabolism*
-
Drosophila
-
Histone Acetyltransferases
-
Humans
-
Models, Molecular
-
Molecular Mimicry*
-
Molecular Sequence Data
-
Nuclear Magnetic Resonance, Biomolecular
-
Nuclear Proteins / chemistry*
-
Nuclear Proteins / metabolism*
-
Protein Structure, Secondary
-
Protein Structure, Tertiary
-
Sequence Alignment
-
Sequence Homology, Amino Acid
-
Solutions
-
TATA Box*
-
TATA-Binding Protein Associated Factors*
-
TATA-Box Binding Protein
-
Transcription Factor TFIID*
-
Transcription Factors / chemistry*
-
Transcription Factors / metabolism*
Substances
-
DNA-Binding Proteins
-
Nuclear Proteins
-
Solutions
-
TATA-Binding Protein Associated Factors
-
TATA-Box Binding Protein
-
Transcription Factor TFIID
-
Transcription Factors
-
Histone Acetyltransferases
-
TATA-binding protein associated factor 250 kDa