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

<div class='caption-title'>Post-translational targeting of SRP substrate YohP is inhibited by (p)ppGpp.</div>
<div class='caption-title'>Co-translational membrane targeting of ribosome-nascent chains (RNCs) is inhibited by (p)ppGpp.</div>
<div class='caption-title'>(p)ppGpp reduces GTPase activity and complex formation of SRP and FtsY.</div>
Czech L, Mais CN, Kratzat H, Sarmah P, Giammarinaro P, Freibert SA, Esser HF, Musial J, Berninghausen O, Steinchen W, Beckmann R, Koch HG, Bange G
OpenAccess logo Nat Commun 13 1069 (2022)
Related entries: 7o9f, 7o9g, 7o9h, 7o9i

Cited: 11 times
EuropePMC logo PMID: 35217658

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.

Reviews citing this publication (4)

  1. Recent advances and perspectives in nucleotide second messenger signaling in bacteria. Hengge R, Pruteanu M, Stülke J, Tschowri N, Turgay K. Microlife 4 uqad015 (2023)
  2. Coping with stress: How bacteria fine-tune protein synthesis and protein transport. Njenga R, Boele J, Öztürk Y, Koch HG. J Biol Chem 299 105163 (2023)
  3. "Metabolic burden" explained: stress symptoms and its related responses induced by (over)expression of (heterologous) proteins in Escherichia coli. Snoeck S, Guidi C, De Mey M. Microb Cell Fact 23 96 (2024)
  4. (p)ppGpp - an important player during heat shock response. Driller K, Cornejo FA, Turgay K. Microlife 4 uqad017 (2023)

Articles citing this publication (7)

  1. mRNA targeting eliminates the need for the signal recognition particle during membrane protein insertion in bacteria. Sarmah P, Shang W, Origi A, Licheva M, Kraft C, Ulbrich M, Lichtenberg E, Wilde A, Koch HG. Cell Rep 42 112140 (2023)
  2. Bacillus subtilis produces (p)ppGpp in response to the bacteriostatic antibiotic chloramphenicol to prevent its potential bactericidal effect. Yang J, Barra JT, Fung DK, Wang JD. mLife 1 101-113 (2022)
  3. Antiplanktonic and Antibiofilm Activity of Rheum palmatum against Streptococcus oralis and Porphyromonas gingivalis. Kommerein N, Vierengel N, Groß J, Opatz T, Al-Nawas B, Müller-Heupt LK. Microorganisms 10 965 (2022)
  4. Transcriptomic Analysis Reveals Key Roles of (p)ppGpp and DksA in Regulating Metabolism and Chemotaxis in Yersinia enterocolitica. Huang C, Li W, Chen J. Int J Mol Sci 24 7612 (2023)
  5. Implication of amino acid metabolism and cell surface integrity for the thermotolerance mechanism in the thermally adapted acetic acid bacterium Acetobacter pasteurianus TH-3. Matsumoto N, Matsutani M, Tanimoto Y, Nakanishi R, Tanaka S, Kanesaki Y, Theeragool G, Kataoka N, Yakushi T, Matsushita K. J Bacteriol 205 e0010123 (2023)
  6. Unraveling the Virulence Factors and Secreted Proteins of an Environmental Isolate Enterobacter sp. S-16. Kumari K, Sharma PK, Singh RP. Curr Microbiol 80 88 (2023)
  7. Control of a chemical chaperone by a universally conserved ATPase. Jiang H, Milanov M, Jüngert G, Angebauer L, Flender C, Smudde E, Gather F, Vogel T, Jessen HJ, Koch HG. iScience 27 110215 (2024)


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