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Related Concept Videos

Allosteric Regulation01:08

Allosteric Regulation

63.5K
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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Ribosomes01:27

Ribosomes

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Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.
Ribosome Structure and Assembly
Ribosomes are composed of ribosomal RNA (rRNA) and proteins. In eukaryotes, rRNA is transcribed from genes in the nucleolus—a part of the nucleus that specializes in ribosome...
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Ribosomes01:27

Ribosomes

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Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.
Ribosome Structure and Assembly
Ribosomes are composed of ribosomal RNA (rRNA) and proteins. In eukaryotes, rRNA is transcribed from genes in the nucleolus—a part of the nucleus that specializes in ribosome...
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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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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

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Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
Ribosome biogenesis begins with the synthesis of 5S and 45S pre-rRNAs by distinct RNA polymerases. The primary transcripts are extensively processed and modified before they are bound and folded by ribosomal proteins and assembly factors,...
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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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The Ribosome as an Allosterically Regulated Molecular Machine.

T M Makarova1, A A Bogdanov

  • 1Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119992, Russia. bogdanov@belozersky.msu.ru.

Biochemistry. Biokhimiia
|March 11, 2018
PubMed
Summary
This summary is machine-generated.

The ribosome, a complex molecular machine, undergoes significant conformational changes during protein synthesis. Allosteric regulation connects distant functional sites, with internal mechanisms controlling translocation, but many details remain unclear.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Ribosomes are essential molecular machines responsible for protein synthesis.
  • Protein synthesis involves complex conformational rearrangements within the ribosome.
  • Allosteric regulation plays a crucial role in coordinating ribosomal functions.

Purpose of the Study:

  • To review and discuss experimental data on the internal consistency of ribosomal conformational rearrangements.
  • To elucidate the mechanisms of allosteric regulation in ribosome operation.
  • To identify knowledge gaps and suggest future research directions.

Main Methods:

  • Förster resonance energy transfer (FRET) for studying translocation dynamics.
  • Chemical probing to map relationships between ribosomal centers.
  • Analysis of existing experimental data on ribosomal conformational changes.

Main Results:

  • Allosteric regulation influences all major stages of ribosome function, linking distant sites.
  • Ribosomal translocation is primarily controlled by internal mechanisms, not ligand positions.
  • Chemical probing reveals connections between decoding, peptidyl transferase, and GTPase centers.

Conclusions:

  • Significant progress has been made in understanding ribosomal allosteric regulation.
  • Many details of ribosomal conformational changes and allosteric mechanisms remain elusive.
  • Novel experimental approaches are required to fully decipher allosteric regulation in ribosomes.