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Related Concept Videos

Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...
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Cis-regulatory sequences are short fragments of non-coding DNA that are present on the same chromosomes as the genes that they regulate. These fragments serve as binding sites for transcriptional regulators, proteins that are responsible for controlling gene transcription and differential gene expression across cell types in eukaryotes. Cis-regulatory sequences can be close to the gene of interest or thousands of bases away in the DNA sequence; however, those sequences that are further away are...
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CD Spectroscopy to Study DNA-Protein Interactions
06:48

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Published on: February 10, 2022

The glucocorticoid receptor dimer interface allosterically transmits sequence-specific DNA signals.

Lisa C Watson1, Kristopher M Kuchenbecker, Benjamin J Schiller

  • 1Tetrad Graduate Program, University of California, San Francisco, California, USA.

Nature Structural & Molecular Biology
|June 4, 2013
PubMed
Summary

Glucocorticoid receptor (GR) binding to DNA involves allosteric signaling between dimer partners. Nonspecific DNA interactions influence GR conformation, affecting gene transcription regulation.

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Area of Science:

  • Molecular biology
  • Structural biology
  • Genetics

Background:

  • Glucocorticoid receptor (GR) regulates gene transcription through DNA binding.
  • The specific DNA sequence bound by GR influences its structure and activity.

Purpose of the Study:

  • To investigate how DNA sequence, particularly non-specific interactions, affects GR conformation and function.
  • To elucidate the allosteric pathway between DNA binding and dimer partner communication.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) chemical-shift difference mapping was used to analyze GR structure.
  • Mutagenesis of the GR dimer interface was performed to study its role in DNA binding and transcription.

Main Results:

  • Nonspecific DNA interactions at specific positions, like the spacer, alter GR DNA-binding domain conformation.
  • These conformational changes affect the DNA-binding surface, lever arm, and dimerization interface.
  • Mutating the dimer interface disrupts the allosteric pathway, altering DNA binding kinetics and transcriptional activity.

Conclusions:

  • GR dimer partners collaborate to interpret DNA shape.
  • This collaboration directs sequence-specific gene activity through an allosteric mechanism.