ArticleJournal of bacteriology2002
FepA with globular domain deletions lacks activity.
Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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The trial behind it
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Who cites it
10 citing papers in PubMed, 34 citations in OpenAlex.
- Permeabilisation of the Outer Membrane of Escherichia coli for Enhanced Transport of Complex Molecules.Microbial biotechnology · 2025Article
- Structural constraints of pyocin S2 import through the ferripyoverdine receptor FpvAI.PNAS nexus · 2024Article
- Going Outside the TonB Box: Identification of Novel FepA-TonB InteractionsJournal of bacteriology · 2017Article
- Regulation of mammalian siderophore 2,5-DHBA in the innate immune response to infection.The Journal of experimental medicine · 2014Article
- Insight from TonB hybrid proteins into the mechanism of iron transport through the outer membrane.Journal of bacteriology · 2008Article
- Evidence of ball-and-chain transport of ferric enterobactin through FepA.The Journal of biological chemistry · 2007Article
- Activities of the Serratia marcescens heme receptor HasR and isolated plug and beta-barrel domains: the beta-barrel forms a heme-specific channel.Journal of bacteriology · 2005Article
- Deletion of the proline-rich region of TonB disrupts formation of a 2:1 complex with FhuA, an outer membrane receptor of Escherichia coli.Protein science : a publication of the Protein Society · 2005Article
- Differential substrate-induced signaling through the TonB-dependent transporter BtuB.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- In vivo reconstitution of the FhuA transport protein of Escherichia coli K-12.Journal of bacteriology · 2003Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
TonB-gated transporters have beta-barrels containing an amino-terminal globular domain that occludes the interior of the barrel. Mutations in the globular domain prevent transport of ligands across the outer membrane. Surprisingly, FepA with deletions of the globular domain (amino acids 3 to 150 and 17 to 150) was previously reported to retain significant sensitivity to colicins B and D and to use ferric enterochelin, all in a TonB-dependent fashion. To further understand TonB interaction with the beta-barrel, in the present study, proteins with deletions of amino acids 1 to 152, 7 to 152, 20 to 152, and 17 to 150 in fepA were constructed and expressed in a deltafepA strain. In contrast to previous studies of fepA globular domain deletions, constructs in this study did not retain sensitivity to colicin B and conferred only marginal sensitivity to colicin D. Consistent with these observations, they failed to bind colicin B and detectably cross-link to TonB in vivo. To address this discrepancy, constructs were tested in other strains, one of which (RWB18-60) did support activity of the FepA globular domain deletion proteins constructed in this study. The characteristics of that strain, as well as the strain in which the deltaFhuA globular domain mutants were seen to be active, suggests the hypothesis that interprotein complementation by two individually nonfunctional proteins restores TonB-dependent activity.
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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.