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

Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

13.6K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
13.6K
Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

5.9K
Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
5.9K
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

3.9K
Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
3.9K
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

3.1K
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...
3.1K
The Electron Transport Chain01:30

The Electron Transport Chain

21.0K
The electron transport chain or oxidative phosphorylation is an exothermic process in which free energy released during electron transfer reactions is coupled to ATP synthesis. This process is a significant source of energy in aerobic cells, and therefore inhibitors of the electron transport chain can be detrimental to the cell's metabolic processes.
Inhibitors of the electron transport chain
Rotenone, a widely used pesticide, prevents electron transfer from Fe-S cluster to ubiquinone or Q...
21.0K
The Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

5.0K
The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria.  In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
5.0K

You might also read

Related Articles

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

Sort by
Same author

SHOC2 Is a Novel Cause of Central Conducting Lymphatic Anomaly.

American journal of medical genetics. Part A·2026
Same author

Scaled Multidimensional Assays of Variant Effect Identify Sequence-Function Relationships in Hypertrophic Cardiomyopathy.

Circulation·2026
Same author

Fmp30p is a mitochondrial phosphatidylinositol hydrolase that modulates CoQ biosynthesis.

Nature communications·2026
Same author

Genetic complementation reveals structure-function links in nodavirus RNA replication complex crowns.

PLoS pathogens·2026
Same author

RBM20 Truncating Variants and Human Cardiomyopathy.

JAMA cardiology·2026
Same author

Neurological manifestations and genotype-phenotype correlations in <i>NDUFAF6</i>-associated mitochondrial disease.

Brain communications·2026

Related Experiment Video

Updated: Mar 16, 2026

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
05:27

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools

Published on: July 20, 2022

2.3K

Mitochondrial Protein Interaction Mapping Identifies Regulators of Respiratory Chain Function.

Brendan J Floyd1, Emily M Wilkerson2, Mike T Veling1

  • 1Morgridge Institute for Research, Madison, WI 53715, USA; Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.

Molecular Cell
|August 9, 2016
PubMed
Summary

Researchers uncovered the functions of unannotated mitochondrial proteins (MXPs) by studying their interactions. This revealed new roles in cellular respiration, including a complex I assembly factor and a coenzyme Q biosynthetic complex.

Keywords:
C15orf48C2orf47DHRS4

More Related Videos

Analysis of the Expression and Complexes Assembly of the Mitochondrial Respiratory Chain Proteins in the Fission Yeast Schizosaccharomyces pombe
08:07

Analysis of the Expression and Complexes Assembly of the Mitochondrial Respiratory Chain Proteins in the Fission Yeast Schizosaccharomyces pombe

Published on: May 2, 2025

1.0K
Author Spotlight: Unveiling Mitochondrial Function and Cellular Metabolic Adaptation in Metabolic Diseases
08:12

Author Spotlight: Unveiling Mitochondrial Function and Cellular Metabolic Adaptation in Metabolic Diseases

Published on: October 4, 2024

2.4K

Related Experiment Videos

Last Updated: Mar 16, 2026

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
05:27

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools

Published on: July 20, 2022

2.3K
Analysis of the Expression and Complexes Assembly of the Mitochondrial Respiratory Chain Proteins in the Fission Yeast Schizosaccharomyces pombe
08:07

Analysis of the Expression and Complexes Assembly of the Mitochondrial Respiratory Chain Proteins in the Fission Yeast Schizosaccharomyces pombe

Published on: May 2, 2025

1.0K
Author Spotlight: Unveiling Mitochondrial Function and Cellular Metabolic Adaptation in Metabolic Diseases
08:12

Author Spotlight: Unveiling Mitochondrial Function and Cellular Metabolic Adaptation in Metabolic Diseases

Published on: October 4, 2024

2.4K

Area of Science:

  • Mitochondrial biology
  • Cellular biochemistry
  • Proteomics

Background:

  • Mitochondria perform vital cellular functions, but many mitochondrial proteins (MXPs) lack defined roles.
  • Understanding MXPs is crucial for elucidating mitochondrial processes and disease mechanisms.

Purpose of the Study:

  • To identify the functions of previously uncharacterized mitochondrial proteins (MXPs).
  • To investigate the roles of MXPs in cellular respiration and mitochondrial complex assembly.

Main Methods:

  • Affinity enrichment mass spectrometry was used to assess condition-specific protein-protein interactions for 50 MXPs.
  • Functional validation of identified MXPs, including C17orf89 and LYRM5, using biochemical assays and genetic disruption.
  • Mapping the topology of a human coenzyme Q biosynthetic complex.

Main Results:

  • MXPs were linked to diverse mitochondrial processes, notably respiratory chain function.
  • C17orf89 was validated as a complex I assembly factor, and its disruption impaired complex I activity.
  • LYRM5 was found to interact with and deflavinate the electron-transferring flavoprotein involved in coenzyme Q biosynthesis.
  • A dynamic human coenzyme Q biosynthetic complex involving multiple MXPs was identified and its topology mapped.

Conclusions:

  • The study provides mechanistic insights into respiratory chain activities and mitochondrial protein function.
  • Identified MXP interactions offer a roadmap for future research into mitochondrial biology and disease.
  • The findings highlight the importance of MXPs in complex I assembly and coenzyme Q metabolism.