ArticleThe Journal of biological chemistry2011
Lipids trigger a conformational switch that regulates signal recognition particle (SRP)-mediated protein targeting.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 43 citations in OpenAlex.
- Article
- Inhibition of SRP-dependent protein secretion by the bacterial alarmone (p)ppGpp.Nature communications · 2022Article
- Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022Review
- The very early evolution of protein translocation across membranes.PLoS computational biology · 2021Article
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- GTP-Dependent FlhF Homodimer Supports Secretion of a Hemolysin inFrontiers in microbiology · 2020Article
- Signal recognition particle binds to translating ribosomes before emergence of a signal anchor sequence.Nucleic acids research · 2017Article
- Article
- Targeting and Insertion of Membrane Proteins.EcoSal Plus · 2017Review
- The Archaeal Signal Recognition Particle: Present Understanding and Future Perspective.Current microbiology · 2017Review
- Electrostatics and Intrinsic Disorder Drive Translocon Binding of the SRP Receptor FtsY.Angewandte Chemie (International ed. in English) · 2016Article
- Mammalian SRP receptor switches the Sec61 translocase from Sec62 to SRP-dependent translocation.Nature communications · 2015Article
- Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon.The Journal of cell biology · 2015Article
- MinD-like ATPase FlhG effects location and number of bacterial flagella during C-ring assembly.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Co-translational protein targeting to the bacterial membrane.Biochimica et biophysica acta · 2014Review
- Regulation of cargo recognition, commitment, and unloading drives cotranslational protein targeting.The Journal of cell biology · 2014Article
- SIMIBI twins in protein targeting and localization.Nature structural & molecular biology · 2013Article
- Signal recognition particle: an essential protein-targeting machine.Annual review of biochemistry · 2013Review
- Dynamic switch of the signal recognition particle from scanning to targeting.Nature structural & molecular biology · 2012Article
- Structural basis for the molecular evolution of SRP-GTPase activation by protein.Nature structural & molecular biology · 2011Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Co-translational protein targeting to the membrane is mediated by the signal recognition particle and its receptor (FtsY). Their homologous GTPase domains interact at the membrane and form a heterodimer in which both GTPases are activated. The prerequisite for protein targeting is the interaction of FtsY with phospholipids. However, the mechanism of FtsY regulation by phospholipids remained unclear. Here we show that the N terminus of FtsY (A domain) is natively unfolded in solution and define the complete membrane-targeting sequence. We show that the membrane-targeting sequence is highly dynamic in solution, independent of nucleotides and directly responds to the density of anionic phospholipids by a random coil-helix transition. This conformational switch is essential for tethering FtsY to membranes and activates the GTPase for its subsequent interaction with the signal recognition particle. Our results underline the dynamics of lipid-protein interactions and their importance in the regulation of protein targeting and translocation across biological membranes.
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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.