Related Experiment Video
Updated: Aug 1, 2026
09:38
Identification of Nucleolar Factors During HIV-1 Replication Through Rev Immunoprecipitation and Mass Spectrometry
Published on: June 26, 2019
TATA element recognition by the TATA box-binding protein has been conserved throughout evolution.
G A Patikoglou1, J L Kim, L Sun
1Laboratories of Molecular Biophysics, Howard Hughes Medical Institute, The Rockefeller University, New York, New York 10021 USA.
Genes & Development
|January 5, 2000
Summary
TATA box-binding protein (TBP) structures reveal conserved binding mechanisms despite promoter variations. This protein-DNA complex structure remains constant in the transcription machinery throughout evolution.
Area of Science:
- Molecular Biology
- Structural Biology
- Genetics
Background:
- The TATA box-binding protein (TBP) is crucial for transcription initiation by RNA polymerase II.
- TBP recognizes the TATA box DNA sequence in core promoter regions.
- Variations in TATA elements can affect transcription initiation efficiency.
Purpose of the Study:
- To determine the cocrystal structures of TBP with various naturally occurring TATA elements.
- To compare these structures with existing TBP-AdMLP TATA box complex structures.
- To elucidate the molecular mechanisms underlying TBP-TATA element complex assembly.
Main Methods:
- X-ray crystallography was used to determine cocrystal structures at high resolution (1.8–2.3 Å).
- Comparative structural analysis of TBP bound to 10 natural TATA elements and the AdMLP TATA box.
- Analysis of protein-DNA interactions and conformational changes.
Main Results:
- Cocrystal structures of TBP with 10 natural TATA elements were determined.
- Minor-groove recognition by TBP induces consistent conformational changes in TATA elements.
- Three mechanisms (transversions, accommodating G, Hoogsteen base pairing) explain diverse TBP-TATA complex formation.
Conclusions:
- The structure of the TBP-TATA box complex is evolutionarily conserved.
- Despite sequence variations, TBP binding induces a stable complex structure.
- Molecular flexibility in TBP-DNA interactions allows recognition of diverse promoter sequences.
More Related Videos
Related Concept Videos
01:49Conserved Binding Sites
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
02:40The Eukaryotic Promoter Region
The eukaryotic promoter region is a segment of DNA located upstream of a gene. It contains an RNA polymerase binding site, a transcription start site, and several cis-regulatory sequences. The proximal promoter region is located in the vicinity of the gene and has cis-regulatory sequences and the core promoter. The core promoter is the binding site for RNA polymerase and is usually located between -35 and +35 nucleotides from the transcription start site. The distal promoter regions are...
01:45Tail-anchoring of Proteins in the ER Membrane
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
01:49Conserved Binding Sites
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
01:30General Transcription Factors
Tissue-specific transcription factors contribute to diverse cellular functions in mammals. For example, the gene for beta globin, a major component of hemoglobin, is present in all cells of the body. However, it is only expressed in red blood cells because the transcription factors that can bind to the promoter sequences of the beta globin gene are only expressed in these cells. Tissue-specific transcription factors also ensure that mutations in these factors may impair only the function of...
01:26Bacterial Translocation and Protein Secretion
Bacterial protein secretion involves translocation systems to ensure proteins reach their designated locations, including the plasma membrane, periplasm, outer membrane, or the external environment. These translocation systems are vital for bacterial physiology, supporting processes like membrane assembly, enzymatic activity in the periplasm, and interactions with the external environment. The division of labor between Sec and Tat pathways ensures efficiency in handling proteins with diverse...