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

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 Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

4.9K
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...
4.9K
Mitochondria01:37

Mitochondria

21.1K
Mitochondria are eukaryotic cellular organelles that are known to produce energy through a process called oxidative phosphorylation. Besides their primary function, mitochondria are involved in various cellular processes, including cell growth, differentiation, signaling, metabolism, and senescence. Age-related changes cause a decline in mitochondrial quality and integrity due to increased mitochondrial mutations and oxidative damage. Thus, aging can severely impact mitochondrial functions,...
21.1K
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 Membranes01:45

Mitochondrial Membranes

17.5K
A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
17.5K
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

19.3K
The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...
19.3K

You might also read

Related Articles

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

Sort by
Same author

When mitochondria lose their fold: matrix proteostasis and stress signaling.

Frontiers in physiology·2026
Same author

Breaking the cycle: from documenting data scarcity to enabling global IBD research.

The lancet. Gastroenterology & hepatology·2026
Same author

Nucleotide-dependent switching and RIPb effector recognition of the barley susceptibility factor RACB.

Communications biology·2026
Same author

Inflammatory bowel disease phenotypes in diverse populations: a global comparative analysis.

Journal of Crohn's & colitis·2026
Same author

Histological approach and differentiation of Crohn's disease and gastrointestinal tuberculosis: Recommendations from the joint IAPM-ISG-CCFI Working Group.

Indian journal of gastroenterology : official journal of the Indian Society of Gastroenterology·2026
Same author

mtHsp70 chaperone converts mitochondrial proteostasis stress into impaired protein import.

Proceedings of the National Academy of Sciences of the United States of America·2026

Related Experiment Video

Updated: Mar 6, 2026

Analyzing Supercomplexes of the Mitochondrial Electron Transport Chain with Native Electrophoresis, In-gel Assays, and Electroelution
08:37

Analyzing Supercomplexes of the Mitochondrial Electron Transport Chain with Native Electrophoresis, In-gel Assays, and Electroelution

Published on: June 1, 2017

14.9K

Chemical Crosslinking in Intact Mitochondria.

Rupa Banerjee1, Umut Günsel1, Dejana Mokranjac2

  • 1Biomedical Center-Physiological Chemistry, LMU Munich, Großhadernerstr. 9, 82152, Martinsried, Germany.

Methods in Molecular Biology (Clifton, N.J.)
|March 10, 2017
PubMed
Summary

Chemical crosslinking in intact yeast mitochondria reveals protein interactions within mitochondrial complexes. This method analyzes ATP-dependent remodeling and identifies specific protein partners for studying mitochondrial function.

Keywords:
CrosslinkingMitochondriaProtein complexProtein-protein interactionsRemodeling of protein complexesTIM23 complex

More Related Videos

Hybrid Clear/Blue Native Electrophoresis for the Separation and Analysis of Mitochondrial Respiratory Chain Supercomplexes
11:25

Hybrid Clear/Blue Native Electrophoresis for the Separation and Analysis of Mitochondrial Respiratory Chain Supercomplexes

Published on: May 19, 2019

14.6K
Author Spotlight: Unveiling Mitochondrial Contact Sites and Architectural Insights
07:55

Author Spotlight: Unveiling Mitochondrial Contact Sites and Architectural Insights

Published on: June 16, 2023

2.1K

Related Experiment Videos

Last Updated: Mar 6, 2026

Analyzing Supercomplexes of the Mitochondrial Electron Transport Chain with Native Electrophoresis, In-gel Assays, and Electroelution
08:37

Analyzing Supercomplexes of the Mitochondrial Electron Transport Chain with Native Electrophoresis, In-gel Assays, and Electroelution

Published on: June 1, 2017

14.9K
Hybrid Clear/Blue Native Electrophoresis for the Separation and Analysis of Mitochondrial Respiratory Chain Supercomplexes
11:25

Hybrid Clear/Blue Native Electrophoresis for the Separation and Analysis of Mitochondrial Respiratory Chain Supercomplexes

Published on: May 19, 2019

14.6K
Author Spotlight: Unveiling Mitochondrial Contact Sites and Architectural Insights
07:55

Author Spotlight: Unveiling Mitochondrial Contact Sites and Architectural Insights

Published on: June 16, 2023

2.1K

Area of Science:

  • Mitochondrial biology
  • Biochemistry
  • Molecular biology

Background:

  • Mitochondrial proteins function in large, multimeric complexes.
  • Analyzing these interactions is crucial for understanding mitochondrial function.
  • Existing methods may not fully capture in vivo interactions within intact organelles.

Purpose of the Study:

  • To describe two chemical crosslinking methods for intact yeast mitochondria.
  • To enable analysis of protein-protein interactions within mitochondrial complexes.
  • To investigate ATP-dependent remodeling and identify crosslinking partners.

Main Methods:

  • Utilizing membrane-permeable crosslinkers on isolated intact yeast mitochondria.
  • Applying two distinct chemical crosslinking protocols.
  • Analyzing protein complex remodeling and specific protein interactions.

Main Results:

  • Successfully crosslinked proteins within intact yeast mitochondria.
  • Demonstrated the ability to study ATP-dependent changes in mitochondrial complexes.
  • Provided a method for identifying specific crosslinking partners of mitochondrial proteins.

Conclusions:

  • Chemical crosslinking in intact mitochondria is effective for studying complex assembly and interactions.
  • These methods allow analysis under various physiological and pathophysiological conditions.
  • The described techniques facilitate deeper understanding of mitochondrial protein interactions.