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Related Concept Videos

Allosteric Regulation01:08

Allosteric Regulation

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...
Allosteric Regulation01:08

Allosteric Regulation

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...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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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Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
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Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Published on: August 9, 2019

Aptamers for allosteric regulation.

Jan L Vinkenborg1, Nora Karnowski, Michael Famulok

  • 1Life & Medical Sciences Institute, Chemical Biology & Medicinal Chemistry Unit, Laboratory of Chemical Biology, Rheinische Friedrich-Wilhelms-Universität Bonn, Bonn, Germany.

Nature Chemical Biology
|July 20, 2011
PubMed
Summary

Nucleic acid aptamers act as allosteric regulators, converting ligand binding into functional output changes. These conformational switching oligonucleotides are key for developing novel aptasensors, aptazymes, and gene regulation tools.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Synthetic Biology
  • Nucleic Acid Chemistry

Background:

  • Aptamers are nucleic acid-based molecules that undergo conformational changes upon ligand binding.
  • These conformational changes can allosterically modulate the function of connected oligonucleotide sequences.
  • This property enables aptamers to function as molecular switches or sensors.

Purpose of the Study:

  • To review recent advancements in the screening, design, and diversity of allosteric aptamers.
  • To discuss the applications of engineered aptasensors and aptazymes.
  • To explore the use of conformational switching oligonucleotides in vitro and for gene expression regulation.

Main Methods:

  • In vitro selection (SELEX) for identifying aptamers with specific binding properties.
  • Engineering of aptamers to create allosteric aptasensors and aptazymes.
  • Design of conformational switching oligonucleotides for diverse applications.

Main Results:

  • Development of a wide range of engineered allosteric aptasensors and aptazymes.
  • Demonstration of aptamer utility in converting specific inputs into altered outputs.
  • Successful application of aptamers as sensors and switches in biochemical assays and living cells.

Conclusions:

  • Allosteric aptamers are versatile tools for molecular sensing and regulation.
  • Recent progress has expanded their screening, design, and application scope.
  • These conformational switching oligonucleotides hold significant potential for biotechnology and synthetic biology.