ArticleThe Journal of cell biology2000
Dissecting the translocase and integrase functions of the Escherichia coli SecYEG translocon.
Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
24 citing papers in PubMed, 69 citations in OpenAlex.
- Functional mapping and engineering of the Sec translocon unlocked by a cell-free system.Science advances · 2026Article
- Article
- mRNA targeting eliminates the need for the signal recognition particle during membrane protein insertion in bacteria.Cell reports · 2023Article
- TheInternational journal of molecular sciences · 2021Article
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Posttranslational insertion of small membrane proteins by the bacterial signal recognition particle.PLoS biology · 2020Article
- Article
- Noncompetitive binding of PpiD and YidC to the SecYEG translocon expands the global view on the SecYEG interactome inThe Journal of biological chemistry · 2019Article
- The bacterial protein YidC accelerates MPIase-dependent integration of membrane proteins.The Journal of biological chemistry · 2019Article
- Cotranslational protein targeting to the membrane: Nascent-chain transfer in a quaternary complex formed at the translocon.Scientific reports · 2018Article
- Driving Forces of Translocation Through Bacterial Translocon SecYEG.The Journal of membrane biology · 2018Article
- The interaction network of the YidC insertase with the SecYEG translocon, SRP and the SRP receptor FtsY.Scientific reports · 2018Article
- The Sec61/SecY complex is inherently deficient in translocating intrinsically disordered proteins.The Journal of biological chemistry · 2017Article
- Lipid dependencies, biogenesis and cytoplasmic micellar forms of integral membrane sugar transport proteins of the bacterial phosphotransferase system.Microbiology (Reading, England) · 2013Review
- Promiscuous targeting of polytopic membrane proteins to SecYEG or YidC by the Escherichia coli signal recognition particle.Molecular biology of the cell · 2012Article
- Visualization of distinct entities of the SecYEG translocon during translocation and integration of bacterial proteins.Molecular biology of the cell · 2009Article
- Diacylglycerol specifically blocks spontaneous integration of membrane proteins and allows detection of a factor-assisted integration.The Journal of biological chemistry · 2008Article
- SecY alterations that impair membrane protein folding and generate a membrane stress.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
- Peculiar properties of DsbA in its export across the Escherichia coli cytoplasmic membrane.Journal of bacteriology · 2005Article
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
Recent evidence suggests that in Escherichia coli, SecA/SecB and signal recognition particle (SRP) are constituents of two different pathways targeting secretory and inner membrane proteins to the SecYEG translocon of the plasma membrane. We now show that a secY mutation, which compromises a functional SecY-SecA interaction, does not impair the SRP-mediated integration of polytopic inner membrane proteins. Furthermore, under conditions in which the translocation of secretory proteins is strictly dependent on SecG for assisting SecA, the absence of SecG still allows polytopic membrane proteins to integrate at the wild-type level. These results indicate that SRP-dependent integration and SecA/SecB-mediated translocation do not only represent two independent protein delivery systems, but also remain mechanistically distinct processes even at the level of the membrane where they engage different domains of SecY and different components of the translocon. In addition, the experimental setup used here enabled us to demonstrate that SRP-dependent integration of a multispanning protein into membrane vesicles leads to a biologically active enzyme.
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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.