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

Protein Folding01:22

Protein Folding

125.9K
Overview
125.9K
Protein Folding01:25

Protein Folding

11.0K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
11.0K
Maxam-Gilbert Sequencing01:05

Maxam-Gilbert Sequencing

12.6K
In the same year as the discovery of the Sanger sequencing method, another group of scientists, Allan Maxam and Walter Gilbert, demonstrated their chemical-cleavage method for DNA sequencing. The Maxam-Gilbert method relies on using different chemicals that can cleave the DNA sequence at specific sites, the separation of resulting DNA fragments of variable size using electrophoresis, and deciphering the DNA sequence from the resulting gel bands.
Challenges of the Maxam-Gilbert Method
The...
12.6K
DNA Base Pairing02:27

DNA Base Pairing

32.8K
Erwin Chargaff’s rules on DNA equivalence paved the way for the discovery of base pairing in DNA. Chargaff’s rules state that in a double-stranded DNA molecule,
32.8K
DNA Base Pairing02:27

DNA Base Pairing

31.4K
31.4K
Protein and Protein Structure02:15

Protein and Protein Structure

86.6K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
86.6K

You might also read

Related Articles

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

Sort by
Same author

NMR-Based Fragment Screening for RNA-Targeted Drug Discovery.

Molecules (Basel, Switzerland)·2026
Same author

Sequence and ionic requirements of pUG fold quadruplexes.

RNA biology·2026
Same author

TDP-43 controls RNA structure through high affinity lattice interactions.

bioRxiv : the preprint server for biology·2025
Same author

PDBe: enhanced structural data exploration to facilitate discovery.

Nucleic acids research·2025
Same author

The structure, folding kinetics, and dynamics of long poly(UG) RNA.

Nucleic acids research·2025
Same author

RNA Modifications and Prp24 Coordinate Lsm2-8 Binding Dynamics during <i>S. cerevisiae</i> U6 snRNP Assembly.

bioRxiv : the preprint server for biology·2025

Related Experiment Video

Updated: Jan 10, 2026

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes
05:37

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes

Published on: April 4, 2025

1.1K

Sequence and ionic requirements of pUG fold quadruplexes.

Saeed Roschdi1, Takuma Kume1, Riley J Petersen1

  • 1Department of Biochemistry, University of Wisconsin-Madison, Madison, WI, USA.

Biorxiv : the Preprint Server for Biology
|November 24, 2025
PubMed
Summary

Poly(UG) repeat RNA forms a specific quadruplex structure, the pUG fold, crucial for RNAi amplification. This fold requires specific ions like potassium and tolerates some sequence variations for stability.

More Related Videos

Author Spotlight: Characterizing DNA G-Quadruplex by Bis-3-Chloropiperidine Based Chemical Mapping
05:32

Author Spotlight: Characterizing DNA G-Quadruplex by Bis-3-Chloropiperidine Based Chemical Mapping

Published on: May 12, 2023

1.8K
Single-molecule Manipulation of G-quadruplexes by Magnetic Tweezers
08:28

Single-molecule Manipulation of G-quadruplexes by Magnetic Tweezers

Published on: September 19, 2017

8.5K

Related Experiment Videos

Last Updated: Jan 10, 2026

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes
05:37

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes

Published on: April 4, 2025

1.1K
Author Spotlight: Characterizing DNA G-Quadruplex by Bis-3-Chloropiperidine Based Chemical Mapping
05:32

Author Spotlight: Characterizing DNA G-Quadruplex by Bis-3-Chloropiperidine Based Chemical Mapping

Published on: May 12, 2023

1.8K
Single-molecule Manipulation of G-quadruplexes by Magnetic Tweezers
08:28

Single-molecule Manipulation of G-quadruplexes by Magnetic Tweezers

Published on: September 19, 2017

8.5K

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Poly(UG) repeat RNA, termed pUG RNA, forms a left-handed parallel quadruplex structure known as the pUG fold.
  • This pUG fold plays a role in RNA interference (RNAi) amplification in *C. elegans* and is found in eukaryotic transcriptomes.

Purpose of the Study:

  • To elucidate the sequence and ionic requirements for pUG RNA folding into the pUG fold.
  • To understand the stability and folding preferences of pUG RNA variants and related sequences.

Main Methods:

  • Investigated sequence variations, including substitutions of uridines and deoxyribose.
  • Assessed the impact of various ions (potassium, sodium, ammonium, magnesium) and polyamines (spermine, spermidine) on pUG fold stability.
  • Examined the influence of flanking sequences on pUG fold formation.

Main Results:

  • The pUG fold requires 12 guanosines but tolerates sequence flexibility, with some variants exhibiting enhanced folding.
  • (GA)12 RNA forms a pUG-like fold with reduced thermodynamic stability compared to (GU)12.
  • The fold tolerates deoxyribose substitutions but not a fully deoxyribose backbone, showing high affinity and specificity for potassium ions.
  • Magnesium ions did not enhance stability, while polyamines slightly decreased it. Surrounding sequences significantly impact folding.

Conclusions:

  • The pUG fold has specific sequence and high potassium ion requirements, with notable tolerance for sequence variations.
  • Understanding these requirements is key for predicting and potentially manipulating pUG fold formation in biological contexts.
  • These findings contribute to a broader understanding of RNA structural dynamics and function.