Signal recognition particle prevents N-terminal processing of bacterial membrane proteins

Nature Communications
Amitabh RanjanWolfgang Wintermeyer

Abstract

Bacterial proteins are synthesized with an N-formylated amino-terminal methionine, and N-formylated peptides elicit innate-immunity responses against bacterial infections. However, the source of these formylated peptides is not clear, as most bacterial proteins are co-translationally deformylated by peptide deformylase. Here we develop a deformylation assay with translating ribosomes as substrates, to show that the binding of the signal recognition particle (SRP) to signal sequences in nascent proteins on the ribosome prevents deformylation, whereas deformylation of nascent proteins without signal sequence is not affected. Deformylation and its inhibition by SRP are not influenced by trigger factor, a chaperone that interacts with nascent chains on the ribosome. We propose that bacterial inner-membrane proteins, in particular those with N-out topology, can retain their N-terminal formyl group during cotranslational membrane insertion and supply formylated peptides during bacterial infections.

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Citations

Nov 2, 2019·Proceedings of the National Academy of Sciences of the United States of America·Chien-I YangShu-Ou Shan
May 10, 2020·FEMS Microbiology Reviews·Daria FijalkowskaPetra Van Damme
Oct 2, 2019·Nature Structural & Molecular Biology·Shuai WangShu-Ou Shan
Nov 25, 2017·Microbiology and Immunology·Jesús A Pérez-AcostaJosé Ángel Huerta-Ocampo
May 24, 2018·FEMS Microbiology Letters·Ruth SteinbergHans-Georg Koch
Jun 12, 2021·Frontiers in Molecular Biosciences·Jiří KoubekGünter Kramer

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Methods Mentioned

BETA
RNaseH
acetylation
ion exchange chromatography

Software Mentioned

Global Kinetic Explorer ( KinTek
FitSpace Editor

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