Proteomics

Dataset Information

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


ABSTRACT: 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 mechanism by which they inactivate ribosomes, it is currently unknown how many different hibernation factors exist. Here, we demonstrate that the YqjD/ElaB/YgaM protein family constitute an abundant class of ribosome-hibernating proteins and represent the first membrane-bound hibernating factors identified in bacteria. Our data demonstrate that they interact with 50S ribosomal subunit and show a concentration-dependent inhibition of protein synthesis. By combining in vivo cross-linking with mass spectrometry, we show that they bind via their N-termini to proteins that surround the ribosomal tunnel exit and even penetrate 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.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Escherichia Coli Bacteria

SUBMITTER: Friedel Drepper  

LAB HEAD: Friedel Drepper

PROVIDER: PXD052307 | Pride | 2025-03-04

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
2022_01_UniProt_ProteomeSet_Ecoli_Isoform.fasta Fasta
ELITE-RSLC034004.raw Raw
ELITE-RSLC034005.raw Raw
ELITE-RSLC034006.raw Raw
ELITE-RSLC034007.raw Raw
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