ArticleProceedings of the National Academy of Sciences of the United States of America1998
Differential use of the signal recognition particle translocase targeting pathway for inner membrane protein assembly in Escherichia coli.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 128 citations in OpenAlex.
- Membrane Protein Insertion in Cells: Principles, Pathways, and Quality Control.Chemical reviews · 2026Review
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Filamentous phages: masters of a microbial sharing economy.EMBO reports · 2019Review
- SecA drives transmembrane insertion of RodZ, an unusual single-span membrane protein.Journal of molecular biology · 2015Article
- Membrane localization of small proteins in Escherichia coli.The Journal of biological chemistry · 2011Article
- Conserved negative charges in the transmembrane segments of subunit K of the NADH:ubiquinone oxidoreductase determine its dependence on YidC for membrane insertion.The Journal of biological chemistry · 2010Article
- Rational design of a fusion partner for membrane protein expression in E. coli.Protein science : a publication of the Protein Society · 2009Article
- The conserved third transmembrane segment of YidC contacts nascent Escherichia coli inner membrane proteins.The Journal of biological chemistry · 2008Article
- An amphiphilic region in the cytoplasmic domain of KdpD is recognized by the signal recognition particle and targeted to the Escherichia coli membrane.Molecular microbiology · 2008Article
- SPdb--a signal peptide database.BMC bioinformatics · 2005Article
- Genome-wide identification of Pseudomonas aeruginosa exported proteins using a consensus computational strategy combined with a laboratory-based PhoA fusion screen.Genome research · 2005Article
- F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis.The Journal of cell biology · 2004Article
- Escherichia coli YidC is a membrane insertase for Sec-independent proteins.The EMBO journal · 2004Article
- Ligand crowding at a nascent signal sequence.The Journal of cell biology · 2003Article
- A conserved function of YidC in the biogenesis of respiratory chain complexes.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Role for both DNA and RNA in GTP hydrolysis by the Neisseria gonorrhoeae signal recognition particle receptor.Journal of bacteriology · 2003Article
- A polytopic membrane protein displays a reversible topology dependent on membrane lipid composition.The EMBO journal · 2002Article
- Functional analysis of the signal recognition particle in Escherichia coli by characterization of a temperature-sensitive ffh mutant.Journal of bacteriology · 2002Article
- YidC, an assembly site for polytopic Escherichia coli membrane proteins located in immediate proximity to the SecYE translocon and lipids.EMBO reports · 2001Article
- Sec-dependent membrane protein insertion: sequential interaction of nascent FtsQ with SecY and YidC.EMBO reports · 2001Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Assembly of several inner membrane proteins-leader peptidase (Lep), a Lep derivative (Lep-inv) that inserts with an inverted topology compared with the wild-type protein, the phage M13 procoat protein, and a procoat derivative (H1-procoat) with the hydrophobic core of the signal peptide replaced by a stretch from the first transmembrane segment in Lep-has been studied in vitro and in Escherichia coli strains that are conditional for the expression of either the 54 homologue (Ffh) or 4.5S RNA, which are the two components of the E. coli signal recognition particle (SRP), or SecE, an essential core component of the E. coli preprotein translocase. Membrane insertion has also been tested in a SecB null strain. Lep, Lep-inv, and H1-procoat require SRP for correct assembly into the inner membrane; in contrast, we find that wild-type procoat does not. Lep and, surprisingly, Lep-inv and H1-procoat fail to insert properly when SecE is depleted, whereas insertion of wild-type procoat is unaffected under these conditions. None of the proteins depend on SecB for assembly. These observations indicate that inner membrane proteins can assemble either by a mechanism in which SRP delivers the protein at the preprotein translocase or by what appears to be a direct integration into the lipid bilayer. The observed change in assembly mechanism when the hydrophobicity of the procoat signal peptide is increased demonstrates that the assembly of an inner membrane protein can be rerouted between different pathways.
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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.