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PreprintCited by 13RNA and protein synthesis mechanismsBacterial Genetics and BiotechnologyToxin Mechanisms and Immunotoxins

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Ribosome-inactivation by a class of widely distributed C-tail anchored membrane proteins

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Njenga, Robert, Boele, Julian, Drepper, Friedel, Sinha, Kasturica, Marouda, Eirini, Huesgen, Pitter F., Blaby-Haas, Crysten, Koch, Hans-Georg·2024·Structure
DOI 10.1101/2024.08.16.608256

Preprint — published as 10.1016/j.str.2024.09.019

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Abstract

Summary: Ribosome hibernation is a commonly used strategy that protects ribosomes under unfavorable conditions and regulates developmental processes. Multiple ribosome-hibernation factors have been identified in all domains of life, but due to their structural diversity and the lack of a common inactivation mechanism, it is currently unknown how many different hibernation factors exist. Here, we show that the YqjD/ElaB/YgaM paralogs, initially discovered as membrane-bound ribosome binding proteins in E. coli, constitute an abundant class of ribosome-hibernating proteins, which are conserved across all proteobacteria and some other bacterial phyla. Our data demonstrate that they inhibit in vitro protein synthesis by interacting with the 50S ribosomal subunit. In vivo cross-linking combined with mass spectrometry reveals their specific interactions with proteins surrounding the ribosomal tunnel exit and even their penetration into the ribosomal tunnel. Thus, YqjD/ElaB/YgaM inhibit translation by blocking the ribosomal tunnel and thus mimic the activity of antimicrobial peptides and macrolide antibiotics.

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Metadata

Authors
Njenga, R., Boele, J., Drepper, F., Sinha, K., Marouda, E., Huesgen, P. F., Blaby-Haas, C., & Koch, H.-G.
Affiliations
University of Freiburg (DE)
Corresponding author
Koch, Hans-Georg
ORCID
Venue
Structure
Publisher
openRxiv
Published
2024-08-17
Volume
32
Issue
12
Pages
2259-2275.e6
ISSN
0969-2126 (ISSN-L)
DOI
10.1101/2024.08.16.608256
OpenAlex
W4403455484
Cited by
13
References
2
Citations by year
2026: 4 · 2025: 7 · 2024: 2
FWCI
1.76
Type
journal article
Language
en
Open access
Licence
Locations
  • Structure (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • eScholarship (California Digital Library) (submittedVersion, cc-by-nc-nd)
  • FreiDok plus (Universitätsbibliothek Freiburg) (submittedVersion)
  • OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
Funders
  • U.S. Department of Energy (-AC02-05CH11231, 05CH11231, DE AC02 05CH11231, DE-AC02-)
  • Joint Genome Institute (AC02-05CH11231, DE–AC02–05CH11231)
  • Deutsche Forschungsgemeinschaft (SFB1381, 278002225, DE-AC02-05CH11231, RTG 2202, SPP 2002, KO2184/9, KO2184/8, 403222702)
  • Office of Science (DEAC02–05CH11231, AC02-05CH11231, DE-AC02)
  • Basic Energy Sciences (DE-AC02, DE-AC02-05CH11231., AC02–05CH11231)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Immunology and Microbiology › Immunology › Toxin Mechanisms and Immunotoxins
Keywords
ribosome inactivation, ribosome hibernation, 50S ribosomal subunit, ribosomal tunnel, protein synthesis inhibition, ribosome-associated proteins, Proteobacteria, antimicrobial peptides, macrolide antibiotics, Escherichia coli
MeSH terms
Bacterial Proteins, Binding Sites, Escherichia coli, Membrane Proteins, Models, Molecular, Protein Binding, Ribosomal Proteins, Ribosomes, Protein Biosynthesis, Escherichia coli Proteins, Ribosome Subunits, Large, Bacterial

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