Protein post-translational modifications in bacteria

Boris Macek*, Karl Forchhammer, Julie Hardouin, Eilika Weber-Ban, Christophe Grangeasse, Ivan Mijakovic

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review


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.
Original languageEnglish
Pages (from-to)651-664
Publication statusPublished - 2019

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