Co-translational protein targeting in bacteria

About 30% of all bacterial proteins execute their function outside of the cytosol and have to be transported into or across the cytoplasmic membrane. Bacteria use multiple protein transport systems in parallel, but the majority of proteins engage two distinct targeting systems. One is the co-transla...

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Bibliographic Details
Published in:FEMS microbiology letters 2018-06, Vol.365 (11)
Main Authors: Steinberg, Ruth, Knüpffer, Lara, Origi, Andrea, Asti, Rossella, Koch, Hans-Georg
Format: Article
Language:English
Subjects:
Adenosine triphosphatase
Bacteria
Cytosol
Membrane proteins
Membranes
Microbiology
Outer membrane proteins
Post-translation
Protein transport
Proteins
Recognition
Signal recognition particle
Substrates
Translation
Translation termination
Translocation
Transportation systems
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Summary:About 30% of all bacterial proteins execute their function outside of the cytosol and have to be transported into or across the cytoplasmic membrane. Bacteria use multiple protein transport systems in parallel, but the majority of proteins engage two distinct targeting systems. One is the co-translational targeting by two universally conserved GTPases, the signal recognition particle (SRP) and its receptor FtsY, which deliver inner membrane proteins to either the SecYEG translocon or the YidC insertase for membrane insertion. The other targeting system depends on the ATPase SecA, which targets secretory proteins, i.e. periplasmic and outer membrane proteins, to SecYEG for their subsequent ATP-dependent translocation. While SRP selects its substrates already very early during their synthesis, the recognition of secretory proteins by SecA is believed to occur primarily after translation termination, i.e. post-translationally. In this review we highlight recent progress on how SRP recognizes its substrates at the ribosome and how the fidelity of the targeting reaction to SecYEG is maintained. We furthermore discuss similarities and differences in the SRP-dependent targeting to either SecYEG or YidC and summarize recent results that suggest that some membrane proteins are co-translationally targeted by SecA.
ISSN:1574-6968
0378-1097
1574-6968
DOI:10.1093/femsle/fny095