Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Ribosome Profiling

Ribosome Profiling

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 helps...

Ribosomal RNA Synthesis

Ribosomal RNA Synthesis

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,...

Ribosomal RNA Synthesis

Ribosomal RNA Synthesis

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,...

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

Conjugated Proteins

Conjugated Proteins

Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
Nucleoproteins are protein complexes that contain nucleic acids, categorized as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs) respectively. The nucleosome is a typical example of a DNP where nuclear DNA is associated with histone proteins. The major antigen for the Covid-19 virus SARS-CoV is an RNP that is critical...

You might also read

Related Articles

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

Sort by

Same author

Monocytic niches escape T cell surveillance and promote Mycobacterium tuberculosis persistence in lymph nodes.

Immunity·2026

Same author

Modulation of Ferroptosis During Early <i>Mycobacterium tuberculosis</i> Infection Contributes to Beijing Lineage Strain SA161 Virulence.

bioRxiv : the preprint server for biology·2026

Same author

Host oxidative stress primes mycobacteria for rapid antibiotic resistance evolution.

Nature communications·2026

Same author

Single-cell profiling reveals that dynamic lung immune responses distinguish protection from susceptibility to tuberculosis.

PLoS pathogens·2026

Same author

A nature-inspired ion trap for parallel manipulation of ions on a massive scale.

Science advances·2026

Same author

High-Resolution Quantification of Two-Way Nanobody Synergy Using Automated Liquid Handling and Computational Modeling.

Bio-protocol·2026

Search research articles

Related Experiment Video

Updated: Jul 11, 2026

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

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

Comprehensive analysis of diverse ribonucleoprotein complexes.

Marlene Oeffinger¹, Karen E Wei, Richard Rogers

¹Rockefeller University, 1230 York Avenue, New York, New York 10021, USA.

|October 9, 2007

Summary

Researchers developed a rapid affinity-purification method to study ribonucleoprotein (RNP) interactions. This new technique efficiently isolates RNP subcomplexes, overcoming previous limitations in yield and sample integrity.

More Related Videos

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

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

Published on: July 10, 2019

Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution

Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution

Published on: January 16, 2017

Related Experiment Videos

Last Updated: Jul 11, 2026

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

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

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

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

Published on: July 10, 2019

Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution

Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution

Published on: January 16, 2017

Area of Science:

Molecular Biology
Biochemistry
Cell Biology

Background:

Studying the dynamic interactome of ribonucleoprotein (RNP) particles is crucial for understanding cellular processes.
Existing methods for RNP complex isolation face limitations like RNA degradation and low yields.

Purpose of the Study:

To develop a novel, rapid affinity-purification method for isolating intact RNP complexes.
To overcome the methodological challenges hindering the study of dynamic RNP interactomes.

Main Methods:

A rapid affinity-purification technique was established for Saccharomyces cerevisiae.
The method focuses on efficient isolation of subcomplexes involved in RNP biogenesis pathways.

Main Results:

The developed method successfully isolates large RNP interactomes.
The technique minimizes RNA degradation and loss of interacting macromolecules.
Achieved near-complete absence of contamination in the isolated complexes.

Conclusions:

This rapid affinity-purification method significantly improves the study of dynamic RNP interactomes.
The technique provides a robust approach for analyzing RNP organization and function.
Enables deeper insights into RNP biogenesis pathways.