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

Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
RNA Structure01:23

RNA Structure

Overview
The basic structure of RNA consists of a five-carbon sugar and one of four nitrogenous bases. 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): messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). All three RNA types consist of a...
RNA Structure01:19

RNA Structure

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...
RNA Structure01:23

RNA Structure

Overview
The basic structure of RNA consists of a five-carbon sugar and one of four nitrogenous bases. 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): messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). All three RNA types consist of a...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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 form...

You might also read

Related Articles

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

Sort by
Same author

Intelligent Veterinary Disease Management Driven by Knowledge Graph for Conservation Breeding of Captive Forest Musk Deer.

Veterinary sciences·2026
Same author

Optimizing the genomic bit budget: an information-theoretic framework for trait-enriched genotyping and stratified screening in <i>Theobroma cacao</i>.

Horticulture research·2026
Same author

Pharmacokinetics, safety, and efficacy of fuzuloparib in combination with abiraterone acetate and prednisone in patients with metastatic castration-resistant prostate cancer: a phase 1 dose escalation and expansion study.

BMC cancer·2026
Same author

Constraining near-term projections of the South Asian high and Afro-Asian summer monsoon rainfall.

Nature communications·2026
Same author

Keypoint-Based Forest Musk Deer Behavioral Recognition Method.

Animals : an open access journal from MDPI·2026
Same author

Affinity Capillary Electrophoresis for the Study of Biomolecular Interactions: Recent Advances and Future Perspectives.

Journal of separation science·2026

Related Experiment Video

Updated: Jun 14, 2026

Sample Preparation for Mass Spectrometry-based Identification of RNA-binding Regions
10:52

Sample Preparation for Mass Spectrometry-based Identification of RNA-binding Regions

Published on: September 28, 2017

OST-HTH: a novel predicted RNA-binding domain.

Vivek Anantharaman1, Dapeng Zhang, L Aravind

  • 1National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.

Biology Direct
|March 23, 2010
PubMed
Summary

Scientists discovered a novel RNA-binding domain in eukaryotic and bacterial proteins involved in ribonucleoprotein (RNP) complex organization. This domain may recognize and localize double-stranded RNA (dsRNA) and is linked to ubiquitination in nuage RNP assembly.

More Related Videos

An Optimized Quantitative Pull-Down Analysis of RNA-Binding Proteins Using Short Biotinylated RNA
07:55

An Optimized Quantitative Pull-Down Analysis of RNA-Binding Proteins Using Short Biotinylated RNA

Published on: February 17, 2023

An Assay for Quantifying Protein-RNA Binding in Bacteria
07:02

An Assay for Quantifying Protein-RNA Binding in Bacteria

Published on: June 12, 2019

Related Experiment Videos

Last Updated: Jun 14, 2026

Sample Preparation for Mass Spectrometry-based Identification of RNA-binding Regions
10:52

Sample Preparation for Mass Spectrometry-based Identification of RNA-binding Regions

Published on: September 28, 2017

An Optimized Quantitative Pull-Down Analysis of RNA-Binding Proteins Using Short Biotinylated RNA
07:55

An Optimized Quantitative Pull-Down Analysis of RNA-Binding Proteins Using Short Biotinylated RNA

Published on: February 17, 2023

An Assay for Quantifying Protein-RNA Binding in Bacteria
07:02

An Assay for Quantifying Protein-RNA Binding in Bacteria

Published on: June 12, 2019

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • The mechanisms governing the organization of ribonucleoprotein (RNP) complexes like polar granules and nuage by proteins such as Oskar and TDRD5/TDRD7 are not well understood.
  • A novel, conserved domain across eukaryotes and bacteria was identified in these proteins.

Purpose of the Study:

  • To investigate the structure and function of a newly identified conserved domain in eukaryotic and bacterial proteins.
  • To explore the potential role of this domain in RNA binding, localization, and RNP complex regulation.

Main Methods:

  • Sequence profile searches to identify conserved domains.
  • Analysis of domain architectures, sequence-structure superpositions, and functional data.
  • Prediction of protein structure and RNA-binding properties.

Main Results:

  • The novel domain is predicted to adopt a winged helix-turn-helix fold, suggesting RNA-binding capabilities, potentially specific for double-stranded RNA (dsRNA).
  • In eukaryotes, this domain is frequently associated with protein-protein or lipid-interaction domains, potentially anchoring proteins to cytoskeletal structures.
  • Fusion of this domain with ubiquitin-binding, E3 ligase, or ubiquitin-like domains suggests a role for ubiquitination in regulating RNP complex assembly and stability.

Conclusions:

  • Proteins containing this domain may play a crucial role in recognizing and localizing dsRNA, including microRNAs (miRNAs), repeat-associated small interfering RNAs (rasiRNAs), and PIWI-interacting RNAs (piRNAs).
  • The domain's association with ubiquitination machinery indicates a significant, previously underappreciated role for ubiquitination in nuage-like RNP complex regulation.
  • A conserved family of proteins in bacteria and eukaryotes combines this predicted RNA-binding domain with a novel domain (DUF88), identified as a potential RNAse.