Protein post-translational modifications in bacteria
Review article, 2019

Over the past decade the number and variety of protein post-translational modifications that have been detected and characterized in bacteria have rapidly increased. Most post-translational protein modifications occur in a relatively low number of bacterial proteins in comparison with eukaryotic proteins, and most of the modified proteins carry low, substoichiometric levels of modification; therefore, their structural and functional analysis is particularly challenging. The number of modifying enzymes differs greatly among bacterial species, and the extent of the modified proteome strongly depends on environmental conditions. Nevertheless, evidence is rapidly accumulating that protein post-translational modifications have vital roles in various cellular processes such as protein synthesis and turnover, nitrogen metabolism, the cell cycle, dormancy, sporulation, spore germination, persistence and virulence. Further research of protein post-translational modifications will fill current gaps in the understanding of bacterial physiology and open new avenues for treatment of infectious diseases.

proteome

ubiquitin

bacterial protein

Author

B. Macek

University of Tübingen

Karl Forchhammer

University of Tübingen

Julie Hardouin

University of Rouen

Eilika Weber-Ban

Swiss Federal Institute of Technology in Zürich (ETH)

C. Grangeasse

Université de Lyon

Ivan Mijakovic

Technical University of Denmark (DTU)

Chalmers, Biology and Biological Engineering, Systems and Synthetic Biology

Nature Reviews Microbiology

1740-1526 (ISSN)

Vol. 17 11 651-664

Subject Categories

Biochemistry and Molecular Biology

Microbiology

Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)

DOI

10.1038/s41579-019-0243-0

PubMed

31485032

More information

Latest update

11/27/2019