Abstract
The spatial and temporal coordination of protein transport is an essential cornerstone of the bacterial adaptation to different environmental conditions. By adjusting the protein composition of extra-cytosolic compartments, like the inner and outer membranes or the periplasmic space, protein transport mechanisms help shaping protein homeostasis in response to various metabolic cues. The universally conserved SecYEG translocon acts at the center of bacterial protein transport and mediates the translocation of newly synthesized proteins into and across the cytoplasmic membrane. The ability of the SecYEG translocon to transport an enormous variety of different substrates is in part determined by its ability to interact with multiple targeting factors, chaperones and accessory proteins. These interactions are crucial for the assisted passage of newly synthesized proteins from the cytosol into the different bacterial compartments. In this review, we summarize the current knowledge about SecYEG-mediated protein transport, primarily in the model organism Escherichia coli, and describe the dynamic interaction of the SecYEG translocon with its multiple partner proteins. We furthermore highlight how protein transport is regulated and explore recent developments in using the SecYEG translocon as an antimicrobial target.
Highlights
The dynamic control of protein synthesis, folding and degradation under different environmental conditions is essential for maintaining a functional proteome in eu- and prokaryotic cells (Mogk et al, 2011; Song et al, 2020)
Prokaryotes lack the sophisticated intracellular organization that is usually observed in eukaryotes, but still maintain distinct compartments like the cytosol, the inner membrane, the periplasm and in Gram-negative bacteria the outer membrane (Figure 1)
Inner membrane proteins are targeted to the SecYEG translocon co-translationally as ribosome-associated nascent chain (RNC) by the signal recognition particle (SRP) pathway (Figure 2; Koch et al, 1999; Beck et al, 2000; Neumann-Haefelin et al, 2000; Akopian et al, 2013b; Steinberg et al, 2018)
Summary
The dynamic control of protein synthesis, folding and degradation under different environmental conditions is essential for maintaining a functional proteome in eu- and prokaryotic cells (Mogk et al, 2011; Song et al, 2020). The SecYEG translocon cooperates with additional protein transport systems (Figure 1), like the YidC insertase
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