ArticleMolecular & cellular proteomics : MCP2012
Novel proteomic tools reveal essential roles of SRP and importance of proper membrane protein biogenesis.
Article in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 101 citations in OpenAlex.
- Double-Labeling Method for Visualization and Quantification of Membrane-Associated Proteins inInternational journal of molecular sciences · 2023Article
- System-wide analyses reveal essential roles of N-terminal protein modification in bacterial membrane integrity.iScience · 2022Article
- Article
- Compensating Complete Loss of Signal Recognition Particle During Co-translational Protein Targeting by the Translation Speed and Accuracy.Frontiers in microbiology · 2021Article
- SecA mediates cotranslational targeting and translocation of an inner membrane protein.The Journal of cell biology · 2017Article
- Impact of chlorhexidine digluconate and temperature on curli production inAIMS microbiology · 2017Article
- Protein folding in the cell envelope of Escherichia coli.Nature microbiology · 2016Review
- Translation elongation regulates substrate selection by the signal recognition particle.The Journal of biological chemistry · 2012Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The signal recognition particle (SRP), which mediates cotranslational protein targeting to cellular membranes, is universally conserved and essential for bacterial and mammalian cells. However, the current understanding of the role of SRP in cell physiology and pathology is still poor, and the reasons behind its essential role in cell survival remain unclear. Here, we systematically analyzed the consequences of SRP loss in E. coli using time-resolved quantitative proteomic analyses. A series of snapshots of the steady-state and newly synthesized proteome unveiled three stages of cellular responses to SRP depletion, and demonstrated essential roles of SRP in metabolism, membrane potential, and protein and energy homeostasis in both the membrane and cytoplasm. We also identified a group of periplasmic proteins, including key molecular chaperones, whose localization was impaired by the loss of SRP; this and additional results showed that SRP is crucial for protein homeostasis in the bacterial envelope. These results reveal the extensive roles that SRP plays in bacterial physiology, emphasize the importance of proper membrane protein biogenesis, and demonstrate the ability of time-resolved quantitative proteomic analysis to provide new biological insights.
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Registered trials
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