Related Experiment Video
Updated: Oct 3, 2025

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
Published on: December 9, 2017
Exceptionally versatile take II: post-translational modifications of lysine and their impact on bacterial physiology
Jürgen Lassak1, Alina Sieber1, Michael Hellwig2
1Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Großhaderner Straße 2-4, D-82152 Planegg, Germany.
Abstract:
Among the 22 proteinogenic amino acids, lysine sticks out due to its unparalleled chemical diversity of post-translational modifications. This results in a wide range of possibilities to influence protein function and hence modulate cellular physiology. Concomitantly, lysine derivatives form a metabolic reservoir that can confer selective advantages to those organisms that can utilize it. In this review, we provide examples of selected lysine modifications and describe their role in bacterial physiology.
More Related Videos
12:49Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
Published on: April 4, 2018
07:26Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
Published on: December 26, 2020
Related Concept Videos
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein....
Histone Modification
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
Bacterial Protein Maturation
Viral Replication: Lysogenic Cycle
Lysogenic Cycle of Bacteriophages
Translational Regulation