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
Histone Modification02:32

Histone Modification

16.9K
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
16.9K
Overview of Fatty Acid Metabolism01:28

Overview of Fatty Acid Metabolism

37.6K
Lipids also are sources of energy that power cellular processes. Like carbohydrates, lipids are composed of carbon, hydrogen, and oxygen, but these atoms are arranged differently. Most lipids are nonpolar and hydrophobic. Major types include fats and oils, waxes, phospholipids, and steroids.
Fatty acids are catabolized in a process called beta-oxidation, which takes place in the matrix of the mitochondria and converts their fatty acid chains into two-carbon units of acetyl groups. The acetyl...
37.6K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

9.9K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
9.9K
Phase II Reactions: Acetylation Reactions01:24

Phase II Reactions: Acetylation Reactions

977
Acetylation, a phase II biotransformation reaction, introduces an acetyl group to drugs or their metabolites. Acetyltransferase enzymes facilitate this reaction, which resembles α-amino acid conjugation due to the addition of a functional group to the drug molecule.
The substrates for acetylation are typically drugs or their metabolites with an amino, sulfonamide, or hydrazine functional group. Acetylation can occur at several points in the drug molecule, including primary, secondary, and...
977
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

You might also read

Related Articles

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

Sort by
Same author

HDA19-mediated deacetylation of histone H3.3 at lysines 27 and 36 regulates plant sensitivity to salt stress.

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

Identification of Potential Proteins Interacting with α-Galactosidase A to Analyze the Pathogenesis of Fabry Disease.

International journal of molecular sciences·2026
Same author

Plants tolerate substantial rates of plastid mistranslation via regulated proteostasis.

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

Author Correction: Regulatory T cells in the mouse hypothalamus control immune activation and ameliorate metabolic impairments in high-calorie environments.

Nature communications·2026
Same author

Dynamic Proximity Networks of Myosin-19 (Myo19) and its Mitochondrial Receptors Miro2 and Metaxin-3.

Molecular & cellular proteomics : MCP·2026
Same author

Heritable transgenerational fitness variation correlates with copper resistance in the clonal duckweed Spirodela polyrhiza.

Proceedings. Biological sciences·2026

Related Experiment Video

Updated: Mar 17, 2026

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
12:49

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Published on: April 4, 2018

12.2K

Lysine acetylation in mitochondria: From inventory to function.

Fabian Hosp1, Ines Lassowskat2, Valeria Santoro3

  • 1Proteomics and Signal Transduction, Max-Planck Institute of Biochemistry, Am Klopferspitz 18, DE-82152 Martinsried, Germany.

Mitochondrion
|August 2, 2016
PubMed
Summary

This review explores how lysine acetylation controls mitochondrial function. Mitochondria have unique conditions that favor acetylation, possibly through non-enzymatic processes. The authors use proteomic data to compare acetylation patterns in plants and animals. They find both shared and species-specific modifications. Acetylation affects key metabolic enzymes and may contribute to disease. The review highlights the need for better tools to study acetylation dynamics. It also stresses the importance of cross-species research to understand acetylation's role in health and disease.

Keywords:
ATP synthaseAcetyl-CoAArabidopsisHumanLysine acetylationMitochondriaMouseRespirationRiceTCA cycleMitochondrial acetylationProteomic techniquesLysine modificationsMetabolic regulation

Frequently Asked Questions

More Related Videos

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
11:08

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

7.4K
Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
14:32

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates

Published on: February 27, 2016

8.7K

Related Experiment Videos

Last Updated: Mar 17, 2026

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
12:49

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Published on: April 4, 2018

12.2K
A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
11:08

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

7.4K
Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
14:32

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates

Published on: February 27, 2016

8.7K

Area of Science:

  • Proteomics in cellular metabolism
  • Post-translational modification biology
  • Mitochondrial biochemistry

Background:

Cells rely on dynamic signaling to adjust to changing environments. Lysine acetylation is a key modification that influences metabolism and signaling. Mitochondria, with their unique chemical environment, show high levels of acetylation. This may be due to acetyl-CoA compartmentalization and high metabolite concentrations. The elevated pH in mitochondria supports non-enzymatic modifications. These factors suggest mitochondria are hotspots for acetylation. Yet, the full regulatory role of acetylation remains unclear. Prior research has shown acetylation affects enzyme activity and metabolic pathways. This gap motivated a broader investigation into mitochondrial acetylation.

Purpose Of The Study:

This review aims to synthesize current knowledge on mitochondrial lysine acetylation. The goal is to explore its functional impact across species. The authors focus on experimental methods for global acetylation analysis. They also examine differences between plant and animal acetylomes. Evolutionary conservation of acetylation is another key focus. Metabolic effects and disease relevance are also considered. The review highlights technical challenges in the field. It emphasizes the need for cross-species and cross-disease knowledge transfer.

Main Methods:

The authors use a literature review approach to compile findings on mitochondrial acetylation. They analyze global proteomic data from mass spectrometry studies. Comparative analysis covers plant and animal acetylomes. Evolutionary patterns of acetylation are explored using bioinformatics. Metabolic effects are inferred from enzyme activity changes. Disease associations are drawn from clinical and model organism studies. Technical challenges are identified through methodological reviews. The synthesis integrates findings from diverse species and experimental models.

Main Results:

Mitochondrial acetylation is widespread and influenced by acetyl-CoA levels. Non-enzymatic modifications are favored by mitochondrial pH and metabolite concentrations. Mass spectrometry has expanded the known acetylome. Plants and animals show both shared and distinct acetylation patterns. Evolutionary conservation suggests functional importance. Acetylation impacts key metabolic enzymes like succinate dehydrogenase. Disease models show altered acetylation in mitochondrial disorders. Technical hurdles include dynamic range and site-specific analysis limitations.

Conclusions:

The authors propose that acetylation is a major regulatory mechanism in mitochondria. They suggest that acetylation affects metabolic flexibility and disease susceptibility. The review highlights the need for better tools to study acetylation dynamics. Cross-species comparisons reveal conserved and divergent acetylation sites. The authors emphasize the importance of integrating proteomic and functional data. They note that non-enzymatic acetylation may be more prevalent than previously thought. The synthesis points to acetylation as a key node in metabolic control. Future work should focus on linking acetylation to specific physiological outcomes.

The authors propose that acetylation regulates mitochondrial metabolism and signaling. It affects enzyme activity and metabolic flexibility.

Mass spectrometry allows global identification of acetylated proteins. It reveals patterns and site-specific modifications across species.

The elevated pH in mitochondria favors non-enzymatic lysine modifications. This may increase acetylation levels independently of acetyltransferases.

Plants and animals share some acetylation sites but show distinct patterns. These differences may reflect species-specific metabolic adaptations.

Altered acetylation is linked to mitochondrial disorders. This suggests a role in disease progression and metabolic dysfunction.

The authors propose better tools for dynamic acetylation analysis. They emphasize the need for cross-species and cross-disease research.