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Ribozymes

Ribozymes

Ribozymes

Ribozymes

The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
Ribozymes can...

Ribosomal RNA Synthesis

Ribosomal RNA Synthesis

Ribosomal RNA Synthesis

Ribosomal RNA Synthesis

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,...

Enzyme Kinetics

Enzyme Kinetics

Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...

Directing Proteins to the Rough Endoplasmic Reticulum

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...

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Related Experiment Video

Updated: Apr 20, 2026

Nanomanipulation of Single RNA Molecules by Optical Tweezers

Nanomanipulation of Single RNA Molecules by Optical Tweezers

Published on: August 20, 2014

Molecular crowding accelerates ribozyme docking and catalysis.

Bishnu P Paudel¹, David Rueda

¹Department of Medicine, Section of Virology, and Single Molecule Imaging Group, MRC-Clinical Sciences Centre, Imperial College London , Du Cane Road, London W12 0NN, U.K.

Journal of the American Chemical Society

|November 18, 2014

Summary

This summary is machine-generated.

Molecular crowding agents, like PEG, stabilize RNA enzymes (ribozymes) by promoting their active structures. This enhances ribozyme folding and catalytic activity, even at lower magnesium ion concentrations.

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Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis

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Published on: July 6, 2021

Area of Science:

Biochemistry
Molecular Biology
RNA Catalysis

Background:

Cellular environments are highly crowded, influencing biomolecular processes.
The impact of molecular crowding on RNA folding and catalysis is not well understood.

Purpose of the Study:

To investigate how molecular crowding affects the folding and catalytic activity of the hairpin ribozyme.
To determine the role of crowding agents in stabilizing active RNA conformations.

Main Methods:

Single-molecule fluorescence resonance energy transfer (smFRET) to monitor RNA structure.
Bulk cleavage assays to measure ribozyme catalytic rates.
Experiments conducted with varying concentrations of polyethylene glycol (PEG) and magnesium ions (Mg2+).

Main Results:

PEG promotes the formation of the ribozyme's active 'docked' conformation by increasing the docking rate.
Magnesium ion-induced folding occurs at significantly lower concentrations in the presence of PEG, nearing physiological levels.
Ribozyme activity increases and its heterogeneity decreases under molecular crowding conditions.

Conclusions:

Molecular crowding plays a crucial role in stabilizing the active conformations of ribozymes.
Crowding agents like PEG can enhance RNA enzyme efficiency in vitro.
Findings suggest molecular crowding is important for ribozyme function in vivo.