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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...
Co-activators and Co-repressors02:04

Co-activators and Co-repressors

Gene transcription is regulated by the synergistic action of several proteins that form a complex at a gene regulatory site. This is observed in eukaryotes, where the regulation of gene expression is a complex process. Regulatory proteins in eukaryotes can broadly be classified into two types – regulators that bind directly to specific DNA sequences and co-regulators that associate with regulatory proteins but cannot directly bind to the DNA. These co-regulators are further divided into...
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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...
Co-activators and Co-repressors02:04

Co-activators and Co-repressors

Gene transcription is regulated by the synergistic action of several proteins that form a complex at a gene regulatory site. This is observed in eukaryotes, where the regulation of gene expression is a complex process. Regulatory proteins in eukaryotes can broadly be classified into two types – regulators that bind directly to specific DNA sequences and co-regulators that associate with regulatory proteins but cannot directly bind to the DNA. These co-regulators are further divided into...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...

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Reverse Yeast Two-hybrid System to Identify Mammalian Nuclear Receptor Residues that Interact with Ligands and/or Antagonists
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Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators.

Stephen J Demarest1, Maria Martinez-Yamout, John Chung

  • 1Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.

Nature
|February 2, 2002
PubMed
Summary
This summary is machine-generated.

Nuclear hormone receptors rely on p160 coactivators and CBP/p300 to regulate gene expression. A novel

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Nuclear hormone receptors are crucial transcription factors regulating vital physiological processes.
  • Hormone response involves p160 coactivators and CBP/p300, which possess histone acetyltransferase activity and remodel chromatin.
  • These coactivators are essential for cell-cycle control, differentiation, apoptosis, and are implicated in diseases like cancer.

Purpose of the Study:

  • To investigate the molecular mechanisms underlying the assembly of the nuclear receptor activation complex.
  • To analyze the structural and thermodynamic interactions between CBP and p160 coactivator domains.

Main Methods:

  • Structural analysis of interaction domains.
  • Thermodynamic analysis of protein-protein interactions.
  • Studying the interplay between CBP and p160 coactivators.

Main Results:

  • Isolated interaction domains of CBP and p160 coactivators are intrinsically disordered.
  • These domains form a high-affinity, cooperatively folded helical heterodimer upon interaction.
  • A mechanism termed 'synergistic folding' was identified, facilitating coactivator recruitment.

Conclusions:

  • Synergistic folding is a novel mechanism for assembling transcriptional activation complexes.
  • This process enables p160 coactivators to recruit CBP/p300, transmitting hormonal signals.
  • Understanding this mechanism provides insights into gene regulation and potential therapeutic targets for related diseases.