Protein post-translational modifications in bacteria
Reviewartikel, 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

Författare

B. Macek

Universität Tübingen

Karl Forchhammer

Universität Tübingen

Julie Hardouin

Universite de Rouen

Eilika Weber-Ban

Eidgenössische Technische Hochschule Zürich (ETH)

C. Grangeasse

Université de Lyon

Ivan Mijakovic

Danmarks Tekniske Universitet (DTU)

Chalmers, Biologi och bioteknik, Systembiologi

Nature Reviews Microbiology

1740-1526 (ISSN)

Vol. 17 11 651-664

Ämneskategorier

Biokemi och molekylärbiologi

Mikrobiologi

Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci)

DOI

10.1038/s41579-019-0243-0

PubMed

31485032

Mer information

Senast uppdaterat

2019-11-27