ArticlePLoS biology2020
Posttranslational insertion of small membrane proteins by the bacterial signal recognition particle.
Article in PLoS biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 32 citations in OpenAlex.
- Membrane Protein Insertion in Cells: Principles, Pathways, and Quality Control.Chemical reviews · 2026Review
- Article
- Article
- Functional diversity and molecular interactions of small membrane proteins in bacteria.microLife · 2025Review
- Review
- MinD-RNase E interplay controls localization of polar mRNAs in E. coli.The EMBO journal · 2024Article
- mRNA targeting eliminates the need for the signal recognition particle during membrane protein insertion in bacteria.Cell reports · 2023Article
- Article
- Little reason to call them small noncoding RNAs.Frontiers in microbiology · 2023Article
- Mapping functional regions of essential bacterial proteins with dominant-negative protein fragments.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Bacterial Small Membrane Proteins: the Swiss Army Knife of Regulators at the Lipid Bilayer.Journal of bacteriology · 2022Review
- Small Proteins; Big Questions.Journal of bacteriology · 2022Article
- Article
- Maturation ofFrontiers in microbiology · 2021Article
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Coupled Transcription-Translation in Prokaryotes: An Old Couple With New Surprises.Frontiers in microbiology · 2020Review
Corrections and comments
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Authors and funding
13 authors at 4 institutions in 4 countries.
Funding
Abstract
Small membrane proteins represent a largely unexplored yet abundant class of proteins in pro- and eukaryotes. They essentially consist of a single transmembrane domain and are associated with stress response mechanisms in bacteria. How these proteins are inserted into the bacterial membrane is unknown. Our study revealed that in Escherichia coli, the 27-amino-acid-long model protein YohP is recognized by the signal recognition particle (SRP), as indicated by in vivo and in vitro site-directed cross-linking. Cross-links to SRP were also observed for a second small membrane protein, the 33-amino-acid-long YkgR. However, in contrast to the canonical cotranslational recognition by SRP, SRP was found to bind to YohP posttranslationally. In vitro protein transport assays in the presence of a SecY inhibitor and proteoliposome studies demonstrated that SRP and its receptor FtsY are essential for the posttranslational membrane insertion of YohP by either the SecYEG translocon or by the YidC insertase. Furthermore, our data showed that the yohP mRNA localized preferentially and translation-independently to the bacterial membrane in vivo. In summary, our data revealed that YohP engages an unique SRP-dependent posttranslational insertion pathway that is likely preceded by an mRNA targeting step. This further highlights the enormous plasticity of bacterial protein transport machineries.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.