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

Protein Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

Intralumenal Vesicles and Multivesicular Bodies

Intralumenal Vesicles and Multivesicular Bodies

Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...

The Supercomplexes in the Crista Membrane

The Supercomplexes in the Crista Membrane

The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...

Overview of Exosomes

Overview of Exosomes

Exosomes are stable, lipid bilayer-enclosed vesicles capable of crossing biological barriers. They can carry a wide range of molecules required for intercellular communication. Once exosomes are released from the cell where they originated, they enter a recipient cell through various pathways such as fusion, receptor-mediated endocytosis, macropinocytosis, and phagocytosis.
Stahl et al. discovered exosomes in 1983, but the exosomes were initially considered waste products released from the...

Protein Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

Structure of Porins

Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...

You might also read

Related Articles

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

Sort by

Same author

Lower third molar surgery - consent and coronectomy.

British dental journal·2016

Same author

Identification of a 60S preribosomal particle that is closely linked to nuclear export.

Molecular cell·2001

Same author

Box C/D small nucleolar RNA trafficking involves small nucleolar RNP proteins, nucleolar factors and a novel nuclear domain.

The EMBO journal·2001

Same author

A nuclear AAA-type ATPase (Rix7p) is required for biogenesis and nuclear export of 60S ribosomal subunits.

The EMBO journal·2001

Same author

The function and synthesis of ribosomes.

Nature reviews. Molecular cell biology·2001

Same author

Maturation and intranuclear transport of pre-ribosomes requires Noc proteins.

Cell·2001

Search research articles

Related Experiment Video

Updated: Jul 17, 2026

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

Musing on the structural organization of the exosome complex.

P Mitchell¹, D Tollervey

¹Wellcome Trust Centre for Cell Biology, ICMB, University of Edinburgh, Kings' Buildings, Edinburgh EH9 3JR, UK. pmitch@holyrood.ed.ac.uk

Nature Structural Biology

|October 4, 2000

Summary

The exosome complex precisely processes or degrades RNA molecules, with RNA helicase cofactors like Mtr4p and Ski2p regulating its function. How the exosome distinguishes between RNA processing and degradation remains unclear.

More Related Videos

Single Particle Electron Microscopy Reconstruction of the Exosome Complex Using the Random Conical Tilt Method

Single Particle Electron Microscopy Reconstruction of the Exosome Complex Using the Random Conical Tilt Method

Published on: March 28, 2011

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

Published on: October 15, 2019

Related Experiment Videos

Last Updated: Jul 17, 2026

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

Single Particle Electron Microscopy Reconstruction of the Exosome Complex Using the Random Conical Tilt Method

Single Particle Electron Microscopy Reconstruction of the Exosome Complex Using the Random Conical Tilt Method

Published on: March 28, 2011

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

Published on: October 15, 2019

Area of Science:

Molecular Biology
RNA Biology
Biochemistry

Background:

The exosome complex, a 3'-->5' exoribonuclease, is crucial for RNA metabolism.
It performs both precise RNA processing and complete RNA degradation.
Key cofactors, including RNA helicases Mtr4p and Ski2p, are essential for exosome activity.

Purpose of the Study:

To review current data on exosome complex function.
To explore how cofactors regulate exosome activity.
To understand how the exosome differentiates between RNA processing and degradation.

Main Methods:

Literature review of existing research on the exosome complex.
Analysis of cofactor roles (Mtr4p, Ski2p) in exosome function.
Discussion of potential structural models for the exosome complex.

Main Results:

Exosome activity is modulated by RNA helicase cofactors.
The mechanism for distinguishing RNA substrates for processing versus degradation is not fully understood.
Speculative models are proposed due to a lack of detailed structural data.

Conclusions:

The exosome complex has dual roles in RNA metabolism.
Cofactor regulation is critical but poorly understood.
Further structural studies are needed to elucidate exosome mechanisms.