Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

The Replisome03:01

The Replisome

DNA replication is carried out by a large complex of proteins that act in a coordinated matter to achieve high-fidelity DNA replication. Together this complex is known as the DNA replication machinery or the replisome.
The synthesis of the leading and lagging strands is a highly coordinated process. To explain this, the “Trombone model” was proposed by Bruce Alberts in 1980. The DNA loop formation starts when a primer is synthesized on the parent lagging strand. The loop grows with the...
The Replisome03:01

The Replisome

DNA replication is carried out by a large complex of proteins that act in a coordinated matter to achieve high-fidelity DNA replication. Together this complex is known as the DNA replication machinery or the replisome.
The synthesis of the leading and lagging strands is a highly coordinated process. To explain this, the “Trombone model” was proposed by Bruce Alberts in 1980. The DNA loop formation starts when a primer is synthesized on the parent lagging strand. The loop grows with the...
Restarting Stalled Replication Forks02:37

Restarting Stalled Replication Forks

DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart, a...
Retrovirus Life Cycles01:10

Retrovirus Life Cycles

Retroviruses have a single-stranded RNA genome that undergoes a special form of replication. Once the retrovirus has entered the host cell, an enzyme called reverse transcriptase synthesizes double-stranded DNA from the retroviral RNA genome. This DNA copy of the genome is then integrated into the host’s genome inside the nucleus via an enzyme called integrase. Consequently, the retroviral genome is transcribed into RNA whenever the host’s genome is transcribed, allowing the retrovirus to...
Viral Replication: Lytic Cycle01:20

Viral Replication: Lytic Cycle

Bacteriophages, or phages, are viruses that specifically infect bacteria. Among them, T-even bacteriophages, such as T4, exhibit a well-characterized lytic replication cycle in Escherichia coli (E. coli). This process ensures the rapid proliferation of the virus while ultimately leading to the destruction of the bacterial host.Attachment and DNA InjectionThe infection process begins with the recognition and binding of the T4 phage to the E. coli cell surface. Tail fibers of the phage...
Replication in Eukaryotes01:29

Replication in Eukaryotes

In eukaryotic cells, DNA replication is highly conserved and tightly regulated. Multiple linear chromosomes must be duplicated with high fidelity before cell division, so there are many proteins that fulfill specialized roles in the replication process. Replication occurs in three phases: initiation, elongation, and termination, and ends with two complete sets of chromosomes in the nucleus.
Many Proteins Orchestrate Replication at the Origin
Eukaryotic replication follows many of the same...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Conserved T cell receptor usage underpins recognition of CD1c presenting a mycobacterial lipid.

bioRxiv : the preprint server for biology·2026
Same author

Next-generation chemogenetic inhibition using a brain-permeant non-prescription agent.

Signal transduction and targeted therapy·2026
Same author

Expression and Purification of Recombinant Macrophage Migration Inhibitory Factor (MIF).

Methods in molecular biology (Clifton, N.J.)·2026
Same author

Expression and Purification of Recombinant D-Dopachrome Tautomerase (D-DT).

Methods in molecular biology (Clifton, N.J.)·2026
Same author

Fragment Screening of MIF by Surface Plasmon Resonance.

Methods in molecular biology (Clifton, N.J.)·2026
Same author

MIF NMR Chemical Shift Perturbation Mapping.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

MLAC: MicroED-assisted ligand structure analysis in complexes and its application to hERG-ligand complexes.

Journal of structural biology·2026
Same journal

Ultrastructural evidence of autophagy-related processes and mitochondrial remodeling in the myxozoan parasite Henneguya piaractus.

Journal of structural biology·2026
Same journal

Architecture and dynamics of a supramolecular oxygen transport system in human homogentisate 1,2-Dioxygenase.

Journal of structural biology·2026
Same journal

Connecting pathways between mineralized fibrocartilage and bone at the Achilles tendon insertion.

Journal of structural biology·2026
Same journal

Structural and functional characterization of thermostable EstS1 esterase for BHET degradation.

Journal of structural biology·2026
Same journal

Following the white rabbit: multiscale 2D3D correlative imaging of bone structure.

Journal of structural biology·2026
See all related articles

Related Experiment Video

Updated: Jun 25, 2026

Electrophoretic Analysis of Replication Through Structure-Prone DNA Repeats Within the SV40-Based Human Episome
05:22

Electrophoretic Analysis of Replication Through Structure-Prone DNA Repeats Within the SV40-Based Human Episome

Published on: September 13, 2024

A picornaviral loop-to-loop replication complex.

Jolyon K Claridge1, Stephen J Headey, John Y H Chow

  • 1Institute of Fundamental Sciences, Massey University, Private Bag 11222, Palmerston North 4442, New Zealand.

Journal of Structural Biology
|March 10, 2009
PubMed
Summary
This summary is machine-generated.

This study models the interaction between picornaviral protease (3Cpro) and viral RNA (5'-UTR SLD). This reveals how RNA binding impacts protease structure and function, crucial for developing new antiviral drugs.

More Related Videos

MicroRNA-based Regulation of Picornavirus Tropism
09:05

MicroRNA-based Regulation of Picornavirus Tropism

Published on: February 6, 2017

Related Experiment Videos

Last Updated: Jun 25, 2026

Electrophoretic Analysis of Replication Through Structure-Prone DNA Repeats Within the SV40-Based Human Episome
05:22

Electrophoretic Analysis of Replication Through Structure-Prone DNA Repeats Within the SV40-Based Human Episome

Published on: September 13, 2024

MicroRNA-based Regulation of Picornavirus Tropism
09:05

MicroRNA-based Regulation of Picornavirus Tropism

Published on: February 6, 2017

Area of Science:

  • Virology
  • Structural Biology
  • Biochemistry

Background:

  • Picornaviruses utilize a conserved mechanism for RNA genome replication.
  • This process involves interaction between the viral protease (3Cpro) and the 5 '-UTR RNA.
  • The 3Cpro catalytic site is a key target for antiviral replication inhibitors.

Purpose of the Study:

  • To determine the first structural model of the complex between picornaviral 3Cpro and a 5 '-UTR RNA element (stem-loop D).
  • To elucidate the binding stoichiometry, shape, and orientation of the 3Cpro-SLD complex.
  • To understand how RNA binding influences the protease's structure and catalytic activity.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) contact information.
  • Small-angle X-ray scattering (SAXS) data.
  • Integration of previous mutagenesis results.

Main Results:

  • A 1:1 binding stoichiometry between 3Cpro and SLD was identified.
  • Key binding determinants involve pronounced loops from both the protease and RNA.
  • RNA binding induces conformational changes in the protease's active site, located distal to the RNA interface.

Conclusions:

  • The structural model provides insights into the picornaviral RNA replication mechanism.
  • Understanding the RNA-protein interaction is vital for designing targeted antiviral therapies.
  • Conformational changes relayed through the protease suggest allosteric regulation of catalytic activity.