Exceptionally versatile take II: post-translational modifications of lysine and their impact on bacterial physiology

Jürgen Lassak; Alina Sieber; Michael Hellwig

doi:10.1515/hsz-2021-0382

Exceptionally versatile take II: post-translational modifications of lysine and their impact on bacterial physiology

Biol Chem. 2022 Feb 17;403(8-9):819-858. doi: 10.1515/hsz-2021-0382. Print 2022 Jul 26.

Authors

Jürgen Lassak¹, Alina Sieber¹, Michael Hellwig²

Affiliations

¹ Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Großhaderner Straße 2-4, D-82152 Planegg, Germany.
² Technische Universität Braunschweig - Institute of Food Chemistry, Schleinitzstraße 20, D-38106 Braunschweig, Germany.

PMID: 35172419
DOI: 10.1515/hsz-2021-0382

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.

Keywords: EF-P modifications; acylation; glycation; methylation; oxidation; pupylation.

Publication types

Review
Research Support, Non-U.S. Gov't

MeSH terms

Amino Acids / metabolism
Bacterial Physiological Phenomena
Lysine* / metabolism
Protein Processing, Post-Translational*
Proteins / metabolism

Substances

Amino Acids
Proteins
Lysine