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

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,...
Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

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...
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

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 precursors...
Mitochondrial Membranes01:45

Mitochondrial Membranes

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,...
Mitochondrial Membranes01:45

Mitochondrial Membranes

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,...
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...

You might also read

Related Articles

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

Sort by
Same author

Eco-Friendly Copper Recovery: Insights to Algal and Agricultural Waste Application.

Water environment research : a research publication of the Water Environment Federation·2026
Same author

Biosynthesis of cerium and gadolinium nanoparticles by Pseudomonas putida KT2440 enables sustainable rare earth elements utilization.

Scientific reports·2026
Same author

Environmental factors modulate the responsiveness and reversibility of the H<sub>2</sub>O<sub>2</sub>-induced inactivation of GAPDH.

Free radical biology & medicine·2026
Same author

Evolution of allostery without shape shifting: Internal dynamics drives functional diversification of a transcriptional repressor superfamily.

bioRxiv : the preprint server for biology·2026
Same author

Comparative evaluation of multiplex bead assay, polymerase chain reaction, and rapid diagnostic test for P. falciparum detection in community surveys in Malawi.

Malaria journal·2026
Same author

PSG6: A mitochondrially-targeted gentisic acid derivative exerts antiplatelet action via mitochondrial complex I inhibition.

Redox biology·2026

Related Experiment Video

Updated: Jun 8, 2026

Nitropeptide Profiling and Identification Illustrated by Angiotensin II
07:31

Nitropeptide Profiling and Identification Illustrated by Angiotensin II

Published on: June 16, 2019

Mitochondrial protein tyrosine nitration.

Laura Castro1, Verónica Demicheli, Verónica Tórtora

  • 1Department of Biochemistry and Center for Free Radical and Biomedical Research, Facultad de Medicina, Universidad de la República, Montevideo, Uruguay.

Free Radical Research
|October 15, 2010
PubMed
Summary

Mitochondria generate reactive species that can modify proteins. This study investigates protein tyrosine nitration in mitochondria, its targets, and how antioxidants can prevent this damage to preserve organelle function.

More Related Videos

Integration of Miniaturized Solid Phase Extraction and LC-MS/MS Detection of 3-Nitrotyrosine in Human Urine for Clinical Applications
08:41

Integration of Miniaturized Solid Phase Extraction and LC-MS/MS Detection of 3-Nitrotyrosine in Human Urine for Clinical Applications

Published on: July 14, 2017

Visualization of Mitochondrial Respiratory Function using Cytochrome C Oxidase / Succinate Dehydrogenase (COX/SDH) Double-labeling Histochemistry
06:53

Visualization of Mitochondrial Respiratory Function using Cytochrome C Oxidase / Succinate Dehydrogenase (COX/SDH) Double-labeling Histochemistry

Published on: November 23, 2011

Related Experiment Videos

Last Updated: Jun 8, 2026

Nitropeptide Profiling and Identification Illustrated by Angiotensin II
07:31

Nitropeptide Profiling and Identification Illustrated by Angiotensin II

Published on: June 16, 2019

Integration of Miniaturized Solid Phase Extraction and LC-MS/MS Detection of 3-Nitrotyrosine in Human Urine for Clinical Applications
08:41

Integration of Miniaturized Solid Phase Extraction and LC-MS/MS Detection of 3-Nitrotyrosine in Human Urine for Clinical Applications

Published on: July 14, 2017

Visualization of Mitochondrial Respiratory Function using Cytochrome C Oxidase / Succinate Dehydrogenase (COX/SDH) Double-labeling Histochemistry
06:53

Visualization of Mitochondrial Respiratory Function using Cytochrome C Oxidase / Succinate Dehydrogenase (COX/SDH) Double-labeling Histochemistry

Published on: November 23, 2011

Area of Science:

  • Biochemistry
  • Cell Biology
  • Mitochondrial Medicine

Background:

  • Mitochondria are central to cellular energy production and reactive species generation.
  • Reactive oxygen and nitrogen species, including peroxynitrite, can cause oxidative damage.
  • Protein tyrosine nitration is a key post-translational modification linked to mitochondrial dysfunction.

Purpose of the Study:

  • To elucidate the biochemical mechanisms of mitochondrial protein tyrosine nitration.
  • To identify primary protein targets of nitration within mitochondria.
  • To analyze the impact of 3-nitrotyrosine formation on mitochondrial structure and function.
  • To evaluate the protective effects of antioxidants against mitochondrial protein nitration.

Main Methods:

  • Biochemical assays to detect and quantify 3-nitrotyrosine.
  • Proteomic analysis to identify nitrated mitochondrial proteins.
  • Functional assays to assess mitochondrial respiration and homeostasis.
  • In vitro and in vivo models of oxidative stress.

Main Results:

  • Established peroxynitrite as a key mediator of mitochondrial protein tyrosine nitration.
  • Identified several key mitochondrial proteins susceptible to nitration, impacting their function.
  • Demonstrated that 3-nitrotyrosine formation disrupts mitochondrial homeostasis.
  • Showed that both endogenous and targeted antioxidants inhibit mitochondrial protein nitration.

Conclusions:

  • Mitochondrial protein tyrosine nitration is a significant contributor to organelle dysfunction.
  • Targeting nitration pathways with antioxidants offers a potential therapeutic strategy.
  • Understanding these mechanisms is crucial for addressing diseases associated with mitochondrial oxidative stress.