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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 be...

Viruses with RNA Genomes

Viruses with RNA Genomes

RNA viruses are categorized into positive-strand, negative-strand, or double-stranded groups based on their genomic structure and replication mechanisms. This classification dictates how they exploit host cellular machinery for protein synthesis and replication. Some RNA viruses also utilize reverse transcription as part of their life cycle, further diversifying their replication strategies.Positive-Strand RNA VirusesPositive-strand RNA viruses have genomes that function directly as messenger...

Inhibitors Of Virion Release

Inhibitors Of Virion Release

Viral replication and dissemination rely on efficient mechanisms for host cell entry, genome replication, assembly, and release. Influenza viruses, such as types A and B, are negative-sense single-stranded RNA viruses with a segmented genome, that depend on two critical surface glycoproteins to carry out these processes: hemagglutinin (HA) and neuraminidase (NA). HA initiates infection by binding to sialic acid residues on the surface of host epithelial cells, facilitating receptor-mediated...

Subviral Agents

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Subviral agents are infectious entities that resemble viruses but lack one or more viral components, such as a capsid or essential replication machinery. These agents include viroids, prions, and satellites, each possessing distinct structural and functional characteristics that influence their mode of infection and replication.Viroids are the simplest subviral agents, consisting of circular, single-stranded RNA molecules without a protein coat. They exclusively infect plants, relying entirely...

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Related Experiment Video

Updated: Jul 3, 2026

DNAzyme 10-23 - Based Nanomachines for Nucleic Acid Recognition

DNAzyme 10-23 - Based Nanomachines for Nucleic Acid Recognition

Published on: February 9, 2024

A virus-based single-enzyme nanoreactor.

Marta Comellas-Aragonès¹, Hans Engelkamp, Victor I Claessen

¹Institute for Molecules and Materials, Radboud University Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands.

Nature Nanotechnology

|July 26, 2008

Summary

This summary is machine-generated.

Researchers developed a new method for single-molecule enzyme studies using virus capsids. This approach avoids surface attachment issues and allows observation of enzyme activity within a confined biological environment.

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Simple and Robust in vivo and in vitro Approach for Studying Virus Assembly

Simple and Robust in vivo and in vitro Approach for Studying Virus Assembly

Published on: March 1, 2012

Area of Science:

Biochemistry
Nanotechnology
Molecular Biology

Background:

Enzyme activity is typically studied at the ensemble level in aqueous solutions.
Single-molecule studies offer deeper insights but often require surface immobilization, risking enzyme denaturation.
Natural enzyme environments involve spatial confinement, influencing their behavior.

Purpose of the Study:

To develop a novel, generic method for single-enzyme studies within a confined environment.
To investigate the enzymatic behavior of horseradish peroxidase (HRP) encapsulated within a virus capsid.
To assess the suitability of virus capsids as nanoreactors for single-molecule enzyme analysis.

Main Methods:

Encapsulation of individual horseradish peroxidase (HRP) enzymes into the cavity of virus capsids.
Performance of single-molecule studies to monitor enzymatic activity.
Analysis of substrate and product permeability through the virus capsid by varying pH.

Main Results:

Successful incorporation of individual HRP enzymes within virus capsids.
Demonstration of enzymatic activity at the single-molecule level within the capsid.
Evidence that virus capsids are permeable to substrates and products.
pH-dependent modulation of capsid permeability was observed.

Conclusions:

Virus capsids provide a viable and natural-like confined environment for single-molecule enzyme studies.
This method overcomes limitations associated with surface immobilization.
The pH-tunable permeability of virus capsids offers potential for controlled nanoreactor applications.