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

Export of Mitochondrial and Chloroplast Genes02:19

Export of Mitochondrial and Chloroplast Genes

4.2K
A eukaryotic cell can have up to three different types of genetic systems: nuclear, mitochondrial, and chloroplast. During evolution, organelles have exported many genes to the nucleus; this transfer is still ongoing in some plant species. Approximately 18% of the Arabidopsis thaliana nuclear genome is thought to be derived from the chloroplast’s cyanobacterial ancestor, and around 75% of the yeast genome derived from the mitochondria’s bacterial ancestor. This export has occurred...
4.2K
Mutations01:39

Mutations

94.5K
Overview
94.5K
Mutations01:35

Mutations

44.6K
Mutations are changes in the sequence of DNA. These changes can occur spontaneously or they can be induced by exposure to environmental factors. Mutations can be characterized in a number of different ways: whether and how they alter the amino acid sequence of the protein, whether they occur over a small or large area of DNA, and whether they occur in somatic cells or germline cells.
Chromosomal Alterations Are Large-Scale Mutations
While point mutations are changes in a single nucleotide in...
44.6K
Animal Mitochondrial Genetics02:59

Animal Mitochondrial Genetics

9.3K
Among all the organelles in an animal cell, only mitochondria have their own independent genomes. Animal mitochondrial DNA is a double-stranded, closed-circular molecule with around 20,000 base pairs. Mitochondrial DNA is unique in that one of its two strands, the heavy, or H, -strand is guanine rich, whereas the complementary strand is cytosine rich and called the light, or L, -strand. Compared to nuclear DNA, mitochondrial DNA has a very low percentage of non-coding regions and is marked by...
9.3K
Protein Complex Assembly02:41

Protein Complex Assembly

16.8K
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...
16.8K
Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

2.5K
Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
2.5K

You might also read

Related Articles

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

Sort by
Same author

Cryo-EM structures of naturally occurring dimeric photosystem II complexes lacking the Mn<sub>4</sub>CaO<sub>5</sub> cluster.

Nature communications·2026
Same author

Structure of E. coli twin-arginine translocase (Tat) complex with bound cargo.

Molecular cell·2026
Same author

Author Correction: SCAF1 drives the compositional diversity of mammalian respirasomes.

Nature structural & molecular biology·2025
Same author

Structure of CFTR bound to (R)-BPO-27 unveils a pore-blockage mechanism.

Nature communications·2025
Same author

The structures of protein kinase A in complex with CFTR: Mechanisms of phosphorylation and noncatalytic activation.

Proceedings of the National Academy of Sciences of the United States of America·2024
Same author

SCAF1 drives the compositional diversity of mammalian respirasomes.

Nature structural & molecular biology·2024

Related Experiment Video

Updated: Feb 7, 2026

The Use of Primary Human Fibroblasts for Monitoring Mitochondrial Phenotypes in the Field of Parkinson's Disease
15:09

The Use of Primary Human Fibroblasts for Monitoring Mitochondrial Phenotypes in the Field of Parkinson's Disease

Published on: October 3, 2012

17.4K

Mammalian Mitochondrial Complex I Structure and Disease-Causing Mutations.

Karol Fiedorczuk1, Leonid A Sazanov2

  • 1Institute of Science and Technology Austria, Am Campus 1, Klosterneuburg 3400, Austria; Present address: The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA.

Trends in Cell Biology
|July 30, 2018
PubMed
Summary

Mitochondrial Complex I, crucial for ATP production, is linked to diseases. New high-resolution cryo-electron microscopy structures reveal its mechanism and assembly, aiding understanding of disease-causing mutations.

Keywords:
NADH–ubiquinone oxidoreductasecryo-electron microscopymitochondrial diseasemitochondrial respiratory chainrespiratory complex I

More Related Videos

Author Spotlight: Establishing a New Fluorescence-Based Protocol for In Vivo Mitochondrial Morphology Analysis in Parkinson's Disease
06:07

Author Spotlight: Establishing a New Fluorescence-Based Protocol for In Vivo Mitochondrial Morphology Analysis in Parkinson's Disease

Published on: June 23, 2023

2.3K
Probing for Mitochondrial Complex Activity in Human Embryonic Stem Cells
12:42

Probing for Mitochondrial Complex Activity in Human Embryonic Stem Cells

Published on: June 17, 2008

14.7K

Related Experiment Videos

Last Updated: Feb 7, 2026

The Use of Primary Human Fibroblasts for Monitoring Mitochondrial Phenotypes in the Field of Parkinson's Disease
15:09

The Use of Primary Human Fibroblasts for Monitoring Mitochondrial Phenotypes in the Field of Parkinson's Disease

Published on: October 3, 2012

17.4K
Author Spotlight: Establishing a New Fluorescence-Based Protocol for In Vivo Mitochondrial Morphology Analysis in Parkinson's Disease
06:07

Author Spotlight: Establishing a New Fluorescence-Based Protocol for In Vivo Mitochondrial Morphology Analysis in Parkinson's Disease

Published on: June 23, 2023

2.3K
Probing for Mitochondrial Complex Activity in Human Embryonic Stem Cells
12:42

Probing for Mitochondrial Complex Activity in Human Embryonic Stem Cells

Published on: June 17, 2008

14.7K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Mitochondrial Complex I is vital for cellular energy production (ATP) via electron transfer and proton translocation.
  • Deficiencies in Complex I are linked to inherited mitochondrial diseases, cancer, aging, and neurodegeneration.
  • Limited understanding of Complex I's molecular mechanisms historically stemmed from a lack of high-resolution structural data.

Purpose of the Study:

  • To elucidate the structural basis of mitochondrial Complex I function and assembly.
  • To provide a structural context for understanding disease-causing mutations in Complex I.
  • To leverage recent advancements in cryo-electron microscopy for near-atomic resolution analysis.

Main Methods:

  • Single particle cryo-electron microscopy (cryo-EM) was employed to determine high-resolution structures of mitochondrial Complex I.
  • Analysis of cryo-EM maps and models to understand enzyme mechanism and assembly processes.
  • Integration of known disease-causing mutations within the determined structural framework.

Main Results:

  • Near-atomic resolution maps and models of mitochondrial Complex I have been recently obtained.
  • These structures offer unprecedented insights into the enzyme's catalytic mechanism and assembly pathways.
  • The structural context for various disease-causing mutations affecting Complex I function has been elucidated.

Conclusions:

  • Recent structural breakthroughs significantly advance the understanding of mitochondrial Complex I.
  • The high-resolution structures provide a foundation for investigating Complex I deficiencies and related diseases.
  • Structural insights are crucial for interpreting the impact of mutations and developing potential therapeutic strategies.