ArticleJournal of bacteriology2004
The core Escherichia coli signal recognition particle receptor contains only the N and G domains of FtsY.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 53 citations in OpenAlex.
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Vanillic acid from Actinidia deliciosa impedes virulence in Serratia marcescens by affecting S-layer, flagellin and fatty acid biosynthesis proteins.Scientific reports · 2017Article
- Article
- Targeting and Insertion of Membrane Proteins.EcoSal Plus · 2017Review
- 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
- SecYEG activates GTPases to drive the completion of cotranslational protein targeting.The Journal of cell biology · 2013Article
- Signal recognition particle: an essential protein-targeting machine.Annual review of biochemistry · 2013Review
- Lipids trigger a conformational switch that regulates signal recognition particle (SRP)-mediated protein targeting.The Journal of biological chemistry · 2011Article
- Genetic evidence for functional interaction of the Escherichia coli signal recognition particle receptor with acidic lipids in vivo.The Journal of biological chemistry · 2010Article
- Lipid activation of the signal recognition particle receptor provides spatial coordination of protein targeting.The Journal of cell biology · 2010Article
- Predominant membrane localization is an essential feature of the bacterial signal recognition particle receptor.BMC biology · 2009Article
- Depletion of the signal recognition particle receptor inactivates ribosomes in Escherichia coli.Journal of bacteriology · 2009Article
- The distinct anchoring mechanism of FtsY from different microbes.Current microbiology · 2009Article
- The membrane-binding motif of the chloroplast signal recognition particle receptor (cpFtsY) regulates GTPase activity.The Journal of biological chemistry · 2009Article
- SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction.Nature structural & molecular biology · 2008Article
- FtsY affects sporulation and antibiotic production by whiH in Streptomyces coelicolor.Current microbiology · 2008Article
- Article
- Conformational changes in the GTPase modules of the signal reception particle and its receptor drive initiation of protein translocation.The Journal of cell biology · 2007Article
- Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites.The Journal of cell biology · 2006Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Previous studies have proposed that the N-terminal A domain (approximately 200 amino acid residues) of the Escherichia coli signal recognition particle (SRP) receptor, FtsY, is required for membrane targeting. In contrast to this suggestion, we show that A domain-truncated versions of FtsY, harboring only domains N and G, are functional. Therefore, we propose that N and G domains constitute the core SRP receptor.
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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.