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

Histone Modification02:32

Histone Modification

14.7K
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...
14.7K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

7.8K
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....
7.8K
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

8.7K
The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
Writers
The writer...
8.7K

You might also read

Related Articles

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

Sort by
Same author

Mechanistic insights on spatiotemporal control of Ras-signaling.

Biological chemistry·2026
Same author

Reprogramming of bacterial virulence by lysine acetylation.

Nature communications·2026
Same author

AcuB senses cellular energy charge to coordinate acetyl-CoA synthesis in bacteria.

Nature communications·2026
Same author

Protein Target Highlights in CASP16: Insights From the Structure Providers.

Proteins·2025
Same author

Insights into a water-mediated catalytic triad architecture in CE20 carbohydrate esterases.

Nature communications·2025
Same author

Staphylococcal SplA and SplB serine proteases target ubiquitin(-like) specific proteases.

AMB Express·2025
Same journal

MRC2 Links Collagen Turnover to Integrin/PI3K/AKT-Driven Fibrogenesis.

Advanced biology·2026
Same journal

Integrative Database-Driven In Silico and In Vitro Study of Anemarrhena asphodeloides Bunge Highlighting Hippeastrine as a Regulator of the HSP90/PI3K/Akt/mTOR Axis in Oral Squamous Cell Carcinoma.

Advanced biology·2026
Same journal

miR-210 in Ischemic Cardiovascular Disease: Functions, Mechanisms, and Therapeutic Potential.

Advanced biology·2026
Same journal

From Spider Webs to Brains: Can the Bri2 BRICHOS Molecular Chaperone Domain Transport Biological Drugs Into the Central Nervous System?

Advanced biology·2026
Same journal

RNAi-Loaded Exosomes for the Management of Breast Cancer: Emerging Paradigms in Precision Therapy.

Advanced biology·2026
Same journal

Cross-Species Transmission and Structural Adaptive Evolution: Implications of the FCoV-23 Pandemic for the Evolution of Coronaviruses.

Advanced biology·2026
See all related articles

Related Experiment Video

Updated: Oct 15, 2025

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
07:26

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli

Published on: December 26, 2020

4.1K

Genetic Code Expansion Tools to Study Lysine Acylation.

Petra Neumann-Staubitz1, Michael Lammers2, Heinz Neumann1

  • 1Department of Chemical Engineering and Biotechnology, University of Applied Sciences Darmstadt, Stephanstrasse 7, 64295, Darmstadt, Germany.

Advanced Biology
|October 29, 2021
PubMed
Summary
This summary is machine-generated.

Lysine acylation, a key protein modification, is increasingly identified but poorly understood. Genetic code expansion (GCE) enables in vivo study of these modifications, revealing their functional roles in diverse biological processes.

Keywords:
chromatincytoskeletongenetic code expansionlysine acylationmetabolism

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

7.2K
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

11.8K

Related Experiment Videos

Last Updated: Oct 15, 2025

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
07:26

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli

Published on: December 26, 2020

4.1K
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

7.2K
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

11.8K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Lysine acylation is a vital post-translational modification regulating protein function, including enzyme activity, localization, and stability.
  • Advances in mass spectrometry have identified thousands of lysine acylation sites across all domains of life, yet their functions remain largely unknown.

Purpose of the Study:

  • To provide an overview of current methods for studying lysine acylation, focusing on genetic code expansion (GCE) for in vivo analysis.
  • To illustrate the potential of GCE and engineered enzymes in elucidating the functional roles of lysine modifications.

Main Methods:

  • Review of state-of-the-art techniques for lysine modification analysis.
  • Application of genetic code expansion (GCE) to install lysine derivatives and photoactivatable amino acids in vivo.
  • Utilizing engineered enzymes for precise installation of lysine modifications.

Main Results:

  • Demonstrated the utility of GCE and engineered enzymes for studying lysine modifications in vivo.
  • Case studies highlight applications in central metabolism, pathogenicity, cytoskeleton, and chromatin dynamics.
  • Provided insights into the dynamic properties and functional significance of acylated lysines.

Conclusions:

  • Genetic code expansion is a powerful tool for investigating the functional roles of lysine acylation in vivo.
  • Understanding lysine acylation dynamics is crucial for deciphering cellular processes and disease mechanisms.
  • This approach opens new avenues for exploring protein function and developing therapeutic strategies.