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Related Concept Videos

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Allosteric Regulation01:08

Allosteric Regulation

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Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
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Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

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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...
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Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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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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Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

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When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
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Mimicking the Function of Signaling Proteins: Toward Artificial Signal Transduction Therapy
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Programming conformational cooperativity to regulate allosteric protein-oligonucleotide signal transduction.

Yuan Liang1,2, Yunkai Qie3,4,5,6, Jing Yang2

  • 1School of Computer Science, Key Lab of High Confidence Software Technologies, Peking University, 100871, Beijing, China.

Nature Communications
|August 14, 2023
PubMed
Summary

Researchers developed a new strategy using conformational signals, not chemical ones, to control molecular networks. This programmable approach regulates gene expression and inhibits tumor cell growth, offering potential for new applications.

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Area of Science:

  • Molecular Biology
  • Synthetic Biology
  • Biochemistry

Background:

  • Conformational cooperativity is a fundamental mechanism in molecular signaling pathways.
  • Developing artificial molecular networks controlled by conformational cooperativity presents significant challenges in programming and controlling structural interactions.

Purpose of the Study:

  • To develop a novel cooperative strategy for regulating protein-oligonucleotide signal transduction using conformational signals.
  • To demonstrate the feasibility of programmable conformational cooperativity for controlling gene expression and inhibiting tumor cell proliferation.

Main Methods:

  • Utilized allosteric DNA constructs to program multiple conformational signals for molecular regulation.
  • Engineered a cooperative regulation mechanism where varying loop lengths induced opposing regulatory effects (down- and up-regulation).
  • Implemented allosteric logic operations using two distinct proteins and validated in cell culture.

Main Results:

  • Successfully generated a cooperative regulation mechanism based on conformational signals.
  • Demonstrated the ability to perform allosteric logic operations with different proteins.
  • Showcased cooperative regulation of PLK1 gene expression in cell culture to inhibit tumor cell proliferation.

Conclusions:

  • The developed programmable conformational cooperativity paradigm offers a new strategy for designing artificial molecular networks.
  • This approach enables precise control over signal transduction and gene expression via conformational changes.
  • The strategy holds potential for applications in synthetic biology, molecular diagnostics, and therapeutic interventions.