Inhibition of SRP-dependent protein secretion by the bacterial alarmone (p)ppGpp

Laura Czech (), Christopher-Nils Mais, Hanna Kratzat, Pinku Sarmah, Pietro Giammarinaro, Sven-Andreas Freibert, Hanna Folke Esser, Joanna Musial, Otto Berninghausen, Wieland Steinchen, Roland Beckmann, Hans-Georg Koch and Gert Bange ()
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Laura Czech: Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry Philipps-Universität Marburg
Christopher-Nils Mais: Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry Philipps-Universität Marburg
Hanna Kratzat: Ludwig-Maximilians-Universität, LMU
Pinku Sarmah: Albert-Ludwigs-Universität Freiburg
Pietro Giammarinaro: Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry Philipps-Universität Marburg
Sven-Andreas Freibert: Philipps-Universität Marburg
Hanna Folke Esser: Ludwig-Maximilians-Universität, LMU
Joanna Musial: Ludwig-Maximilians-Universität, LMU
Otto Berninghausen: Ludwig-Maximilians-Universität, LMU
Wieland Steinchen: Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry Philipps-Universität Marburg
Roland Beckmann: Ludwig-Maximilians-Universität, LMU
Hans-Georg Koch: Albert-Ludwigs-Universität Freiburg
Gert Bange: Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry Philipps-Universität Marburg

Nature Communications, 2022, vol. 13, issue 1, 1-14

Abstract: Abstract The stringent response enables bacteria to respond to nutrient limitation and other stress conditions through production of the nucleotide-based second messengers ppGpp and pppGpp, collectively known as (p)ppGpp. Here, we report that (p)ppGpp inhibits the signal recognition particle (SRP)-dependent protein targeting pathway, which is essential for membrane protein biogenesis and protein secretion. More specifically, (p)ppGpp binds to the SRP GTPases Ffh and FtsY, and inhibits the formation of the SRP receptor-targeting complex, which is central for the coordinated binding of the translating ribosome to the SecYEG translocon. Cryo-EM analysis of SRP bound to translating ribosomes suggests that (p)ppGpp may induce a distinct conformational stabilization of the NG domain of Ffh and FtsY in Bacillus subtilis but not in E. coli.

Date: 2022
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DOI: 10.1038/s41467-022-28675-0

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