ArticleThe EMBO journal2000
Anionic phospholipids are involved in membrane association of FtsY and stimulate its GTPase activity.
Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 148 citations in OpenAlex.
- mRNA targeting eliminates the need for the signal recognition particle during membrane protein insertion in bacteria.Cell reports · 2023Article
- Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022Review
- Fidelity of Cotranslational Protein Targeting to the Endoplasmic Reticulum.International journal of molecular sciences · 2021Review
- Receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER.Science advances · 2021Article
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- GTP-Dependent FlhF Homodimer Supports Secretion of a Hemolysin inFrontiers in microbiology · 2020Article
- Understanding the antimicrobial properties/activity of an 11-residue Lys homopeptide by alanine and proline scan.Amino acids · 2018Article
- Activation of ROP6 GTPase by Phosphatidylglycerol in Arabidopsis.Frontiers in plant science · 2018Article
- Article
- Targeting and Insertion of Membrane Proteins.EcoSal Plus · 2017Review
- Anionic Phospholipids and the Albino3 Translocase Activate Signal Recognition Particle-Receptor Interaction during Light-harvesting Chlorophyll a/b-binding Protein Targeting.The Journal of biological chemistry · 2017Article
- ATPase and GTPase Tangos Drive Intracellular Protein Transport.Trends in biochemical sciences · 2016Review
- Electrostatics and Intrinsic Disorder Drive Translocon Binding of the SRP Receptor FtsY.Angewandte Chemie (International ed. in English) · 2016Article
- Dynamics of co-translational protein targeting.Current opinion in chemical biology · 2015Review
- Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon.The Journal of cell biology · 2015Article
- Co-translational protein targeting to the bacterial membrane.Biochimica et biophysica acta · 2014Review
- SIMIBI twins in protein targeting and localization.Nature structural & molecular biology · 2013Article
- SecYEG activates GTPases to drive the completion of cotranslational protein targeting.The Journal of cell biology · 2013Article
- Intra-plastid protein trafficking: how plant cells adapted prokaryotic mechanisms to the eukaryotic condition.Biochimica et biophysica acta · 2013Review
- Signal recognition particle: an essential protein-targeting machine.Annual review of biochemistry · 2013Review
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
FtsY, the Escherichia coli homologue of the eukaryotic signal recognition particle (SRP) receptor alpha-subunit, is located in both the cytoplasm and inner membrane. It has been proposed that FtsY has a direct targeting function, but the mechanism of its association with the membrane is unclear. FtsY is composed of two hydrophilic domains: a highly charged N-terminal domain (the A-domain) and a C-terminal GTP-binding domain (the NG-domain). FtsY does not contain any hydrophobic sequence that might explain its affinity for the inner membrane, and a membrane-anchoring protein has not been detected. In this study, we provide evidence that FtsY interacts directly with E.coli phospholipids, with a preference for anionic phospholipids. The interaction involves at least two lipid-binding sites, one of which is present in the NG-domain. Lipid association induced a conformational change in FtsY and greatly enhanced its GTPase activity. We propose that lipid binding of FtsY is important for the regulation of SRP-mediated protein targeting.
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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.