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

Ribosome Profiling02:24

Ribosome Profiling

4.0K
Ribosome profiling or ribo-sequencing is a deep sequencing technique that produces a snapshot of active translation in a cell. It selectively sequences the mRNAs protected by ribosomes to get an insight into a cell’s translation landscape at any given point in time.
Applications of ribosome profiling
Ribosome profiling has many applications, including in vivo monitoring of translation inside a particular organ or tissue type and quantifying new protein synthesis levels.
The technique...
4.0K
Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

14.5K
Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
Ribosome biogenesis begins with the synthesis of 5S and 45S pre-rRNAs by distinct RNA polymerases. The primary transcripts are extensively processed and modified before they are bound and folded by ribosomal proteins and assembly factors,...
14.5K
The Nucleolus02:55

The Nucleolus

10.2K
The nucleolus is the most prominent substructure of the nucleus. When it was first discovered, it was considered to be an isolated organelle that forms fibrils and granules. In 1931, the relationship between the nucleolus and chromosomes was first described by Heitz. He observed that the appearance and size of nucleolus varies depending on the stage of the cell cycle. He also noticed constricted regions on different chromosomes clustered together at definite cell cycle stages. These regions,...
10.2K

You might also read

Related Articles

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

Sort by
Same author

Identification of Novel Interacting Proteins of FUZ and GPR161.

Proteomics·2026
Same author

Agnostic material classification using differential de Bruijn graphs of DNA imprints.

bioRxiv : the preprint server for biology·2026
Same author

Evaluation of a method for affinity measurement using solution equilibrium titration with magnetic beads.

Analytical biochemistry·2026
Same author

Identifying membrane-bound transcriptional regulatory proteins from rare but evolutionarily conserved domain combinations.

Nucleic acids research·2026
Same author

Single-Molecule Visualization of DNase I-Mediated DNA Cleavage by High-Speed Atomic Force Microscopy.

ACS chemical biology·2026
Same author

A cross-vertebrate brain protein interaction map identifies conserved neural and non-neural complexes.

Cell reports·2026

Related Experiment Video

Updated: Jan 4, 2026

Method for the Isolation and Identification of mRNAs, microRNAs and Protein Components of Ribonucleoprotein Complexes from Cell Extracts using RIP-Chip
13:34

Method for the Isolation and Identification of mRNAs, microRNAs and Protein Components of Ribonucleoprotein Complexes from Cell Extracts using RIP-Chip

Published on: September 29, 2012

28.0K

Systematic Discovery of Endogenous Human Ribonucleoprotein Complexes.

Anna L Mallam1, Wisath Sae-Lee1, Jeffrey M Schaub1

  • 1Department of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712, USA; Center for Systems and Synthetic Biology, University of Texas at Austin, Austin, TX 78712, USA; Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA.

Cell Reports
|October 31, 2019
PubMed
Summary
This summary is machine-generated.

Researchers developed a new proteomics method to identify ribonucleoprotein (RNP) complexes in human cells. This study reveals that over 20% of human protein complexes associate with RNA, uncovering new insights into RNA-protein interactions.

Keywords:
DIF-FRACRBPRNA-binding proteinRNPbiochemical fractionationinteractomemass spectrometryprotein complexesproteomicsribonucleoprotein complex

More Related Videos

A Rapid High-throughput Method for Mapping Ribonucleoproteins RNPs on Human pre-mRNA
13:00

A Rapid High-throughput Method for Mapping Ribonucleoproteins RNPs on Human pre-mRNA

Published on: December 2, 2009

12.2K
Identification of Footprints of RNA:Protein Complexes via RNA Immunoprecipitation in Tandem Followed by Sequencing RIPiT-Seq
09:26

Identification of Footprints of RNA:Protein Complexes via RNA Immunoprecipitation in Tandem Followed by Sequencing RIPiT-Seq

Published on: July 10, 2019

11.1K

Related Experiment Videos

Last Updated: Jan 4, 2026

Method for the Isolation and Identification of mRNAs, microRNAs and Protein Components of Ribonucleoprotein Complexes from Cell Extracts using RIP-Chip
13:34

Method for the Isolation and Identification of mRNAs, microRNAs and Protein Components of Ribonucleoprotein Complexes from Cell Extracts using RIP-Chip

Published on: September 29, 2012

28.0K
A Rapid High-throughput Method for Mapping Ribonucleoproteins RNPs on Human pre-mRNA
13:00

A Rapid High-throughput Method for Mapping Ribonucleoproteins RNPs on Human pre-mRNA

Published on: December 2, 2009

12.2K
Identification of Footprints of RNA:Protein Complexes via RNA Immunoprecipitation in Tandem Followed by Sequencing RIPiT-Seq
09:26

Identification of Footprints of RNA:Protein Complexes via RNA Immunoprecipitation in Tandem Followed by Sequencing RIPiT-Seq

Published on: July 10, 2019

11.1K

Area of Science:

  • Molecular Biology
  • Proteomics
  • Biochemistry

Background:

  • RNA-binding proteins (RBPs) are crucial for cellular functions and implicated in human diseases.
  • Previous research focused on individual RBPs, neglecting their assembly into higher-order ribonucleoprotein (RNP) complexes.

Purpose of the Study:

  • To systematically identify RNP complexes in human cells using a novel proteomics approach.
  • To investigate the role of RNA in the assembly and stability of protein complexes.
  • To create a comprehensive resource for exploring RNA-associated proteins.

Main Methods:

  • Development and application of a proteomics method for identifying RNP complexes.
  • Analysis of protein complex composition and stability in the presence and absence of RNA.
  • Systematic identification of cell-type-specific RNA-associated proteins in mouse embryonic stem cells.

Main Results:

  • Identification of 1,428 RNA-associated protein complexes, with over 20% of known human protein complexes containing RNA.
  • Characterization of complexes that dissociate, change composition, or form protein-only structures without RNA.
  • Creation of the rna.MAP online resource (rna.proteincomplexes.org) for accessing identified complexes.

Conclusions:

  • The study provides a robust methodology for systematic RNP complex identification across various biological contexts.
  • RNA plays a significant role in the assembly and regulation of a substantial portion of the human proteome.
  • The rna.MAP resource facilitates future research into RNA-protein interactions in human tissues, diseases, and diverse organisms.