Abstract
The TATA box-binding protein (TBP) is required by all three eukaryotic RNA polymerases for correct initiation of transcription of ribosomal, messenger, small nuclear, and transfer RNAs. The cocrystal structure of the C-terminal/core region of human TBP complexed with the TATA element of the adenovirus major late promoter has been determined at 1.9 angstroms resolution. Structural and functional analyses of the protein-DNA complex are presented, with a detailed comparison to our 1.9-angstroms resolution structure of Arabidopsis thaliana TBP2 bound to the same TATA box.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Arabidopsis / chemistry
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Base Sequence
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Conserved Sequence
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Crystallography, X-Ray
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DNA / chemistry
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DNA / genetics
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DNA-Binding Proteins / chemistry*
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism
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Humans
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Models, Molecular
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Molecular Sequence Data
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Molecular Structure
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Nucleic Acid Conformation
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Plant Proteins / chemistry
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Protein Conformation
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TATA Box*
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TATA-Box Binding Protein
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Transcription Factors / chemistry*
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Transcription Factors / genetics
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Transcription Factors / metabolism
Substances
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DNA-Binding Proteins
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Plant Proteins
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TATA-Box Binding Protein
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Transcription Factors
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DNA