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

piRNA - Piwi-interacting RNAs02:57

piRNA - Piwi-interacting RNAs

7.5K
PIWI-interacting RNAs, or piRNAs, are the most abundant short non-coding RNAs. More than 20,000 genes have been found in humans that code for piRNAs while only 2000 genes have been found for miRNAs. piRNAs can act at the transcriptional and post-transcriptional levels and have a vital role in silencing transposable elements present in germ cells. They are also involved in epigenetic silencing and activation. Previously, they were thought to function only in germ cells but new evidence suggests...
7.5K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

14.1K
Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
14.1K
RNA Interference01:23

RNA Interference

27.8K
RNA interference (RNAi) is a process in which a small non-coding RNA molecule blocks the post-transcriptional expression of a gene by binding to its messenger RNA (mRNA) and preventing the protein from being translated.
This process occurs naturally in cells, often through the activity of genomically-encoded microRNAs. Researchers can take advantage of this mechanism by introducing synthetic RNAs to deactivate specific genes for research or therapeutic purposes. For example, RNAi could be used...
27.8K
Protein-protein Interfaces02:04

Protein-protein Interfaces

14.4K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.4K
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

10.1K
Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
10.1K
RNA Structure01:19

RNA Structure

7.2K
The basic structure of RNA consists of a string of ribonucleotides attached by phosphodiester bonds. Although most RNA is single-stranded, it can form complex secondary and tertiary structures. Such structures play essential roles in the regulation of transcription and translation.
Different Types of RNA Have the Same Basic Structure
There are three main types of ribonucleic acid (RNA) involved in protein synthesis: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). All three...
7.2K

You might also read

Related Articles

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

Sort by
Same author

Correction: <i>In situ</i> formation of transcriptional modulators using non-canonical DNA i-motifs.

Chemical science·2026
Same author

Integrated NMR/MD investigation reveals differences after reweighting in conformational ensembles of GAAG and GCAA tetraloops.

RNA (New York, N.Y.)·2026
Same author

RNA•DNA:DNA Triplex Formation Modulates Individual Base Pair Stabilities in the DNA Target Duplex.

RNA (New York, N.Y.)·2026
Same author

Moving NMR infrastructures to remote access capabilities.

Progress in nuclear magnetic resonance spectroscopy·2026
Same author

Structure and sequence characteristics of 5'-stem-loop 1 modulate the escape from nsp1-mediated repression in SARS-CoV-2 variants.

Nucleic acids research·2026
Same author

Dissecting the Chemical and Thermal Stabilities of Tetrads in G-Quadruplexes to Derive a Structure-Activity Relation for a Thrombin-Binding DNA G-Quadruplex Aptamer.

Chembiochem : a European journal of chemical biology·2026
Same journal

Structure of Perinereis linea erythrocruorin reveals a compact extracellular globin megacomplex.

Structure (London, England : 1993)·2026
Same journal

Meet the author: Stephen Brohawn.

Structure (London, England : 1993)·2026
Same journal

Tetraspanins bring Norrin into focus: Structural insights into ligand-specific Wnt signaling.

Structure (London, England : 1993)·2026
Same journal

Uncovering subtype-selective activation of the K<sub>Ca</sub>3.1 channel by SKA-111.

Structure (London, England : 1993)·2026
Same journal

Identification and structure determination of a type III-Bv CRISPR complex that post-translationally modifies an associated toxin.

Structure (London, England : 1993)·2026
Same journal

Cryo-EM structure of the Arabidopsisthaliana ribosome in translating and non-translating states.

Structure (London, England : 1993)·2026
See all related articles

Related Experiment Video

Updated: Jan 18, 2026

In Vivo Proximity Biotinylation for Protein Interaction Studies in Paramecium tetraurelia
06:43

In Vivo Proximity Biotinylation for Protein Interaction Studies in Paramecium tetraurelia

Published on: September 12, 2025

1.1K

Double take on Piwi protein/piRNA complex structure.

Harald Schwalbe1

  • 1Institute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance, Johann Wolfgang Goethe-University, Frankfurt a. M., Max-von-Laue-Straße 7, D-60438, Frankfurt, Germany. schwalbe@nmr.uni-frankfurt.de

Structure (London, England : 1993)
|February 9, 2011
PubMed
Summary
This summary is machine-generated.

Two studies reveal highly similar structures of Piwi PAZ domains bound to PIWI-interacting RNAs (piRNAs). These findings, using NMR spectroscopy and X-ray crystallography, advance our understanding of small RNA pathways.

More Related Videos

In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay
08:56

In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay

Published on: May 5, 2020

6.3K
Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids
09:04

Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids

Published on: September 21, 2017

9.9K

Related Experiment Videos

Last Updated: Jan 18, 2026

In Vivo Proximity Biotinylation for Protein Interaction Studies in Paramecium tetraurelia
06:43

In Vivo Proximity Biotinylation for Protein Interaction Studies in Paramecium tetraurelia

Published on: September 12, 2025

1.1K
In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay
08:56

In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay

Published on: May 5, 2020

6.3K
Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids
09:04

Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids

Published on: September 21, 2017

9.9K

Area of Science:

  • Structural biology
  • Molecular biology
  • Biochemistry

Background:

  • Two independent research groups, Carlomagno/Pillai labs and the Patel group, have elucidated the structures of Piwi PAZ domains complexed with piRNA.
  • These studies employed complementary structural biology techniques: Nuclear Magnetic Resonance (NMR) spectroscopy and X-ray crystallography.

Discussion:

  • Both studies independently determined highly similar three-dimensional structures of the Piwi PAZ-piRNA complexes.
  • The structural data obtained by NMR and X-ray crystallography exhibit comparable resolution, validating the findings.

Key Insights:

  • The structural convergence from distinct methodologies underscores the conserved nature of Piwi PAZ domain-piRNA interactions.
  • These high-resolution structures provide critical insights into the molecular mechanisms governing piRNA binding and the function of the Piwi Argonaut protein family.

Outlook:

  • Further structural and functional studies can build upon these foundational results to explore the dynamics and regulatory roles of Piwi-piRNA complexes in gene silencing.
  • These insights are crucial for understanding RNA-mediated gene regulation and developing novel therapeutic strategies targeting small RNA pathways.