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

Czech, L., Mais, C. N., Kratzat, H., Sarmah, P., Giammarinaro, P., Freibert, S. A., et al. (2022). Inhibition of SRP-dependent protein secretion by the bacterial alarmone (p)ppGpp. Nature Communications, 13(1): 1069. doi:10.1038/s41467-022-28675-0.

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https://doi.org/10.1038/s41467-022-28675-0 (Publisher version)
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Verlagsversion
OA-Status:
Gold

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 Creators:
Czech, L., Author
Mais, C. N., Author
Kratzat, H., Author
Sarmah, P., Author
Giammarinaro, P., Author
Freibert, S. A., Author
Esser, H. F., Author
Musial, J., Author
Berninghausen, O., Author
Steinchen, W., Author
Beckmann, R., Author
Koch, H. G., Author
Bange, G.1, Author           
Affiliations:
1Max Planck Fellow Molecular Physiology of Microbes, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3321791              

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 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.

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Language(s): eng - English
 Dates: 2022-02-27
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: Other: 35217658
DOI: 10.1038/s41467-022-28675-0
ISSN: 2041-1723 (Electronic)2041-1723 (Linking)
 Degree: -

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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 13 (1) Sequence Number: 1069 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723