ArticleJournal of bacteriology2005
Peculiar properties of DsbA in its export across the Escherichia coli cytoplasmic membrane.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Exploration of Length and Hydrophobicity Requirements for Optimal α-Amylase Secretion in Bacillus subtilis Based on Rational Design.Microbial biotechnology · 2026Article
- Analysis of the Brucella suis Twin Arginine Translocation System and Its Substrates Shows That It Is Essential for Viability.Infection and immunity · 2023Article
- Ribosome profiling reveals multiple roles of SecA in cotranslational protein export.Nature communications · 2022Article
- Article
- Signal recognition particle and SecA cooperate during export of secretory proteins with highly hydrophobic signal sequences.PloS one · 2014Article
- Emerging themes in SecA2-mediated protein export.Nature reviews. Microbiology · 2012Review
- YidC is involved in the biogenesis of the secreted autotransporter hemoglobin protease.The Journal of biological chemistry · 2010Article
- Sequential translocation of an Escherchia coli two-partner secretion pathway exoprotein across the inner and outer membranes.Molecular microbiology · 2010Article
- Signal recognition particle-dependent inner membrane targeting of the PulG Pseudopilin component of a type II secretion system.Journal of bacteriology · 2007Article
- SecY alterations that impair membrane protein folding and generate a membrane stress.The Journal of cell biology · 2007Article
- The bacterial twin-arginine translocation pathway.Annual review of microbiology · 2006Review
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Export of DsbA, a protein disulfide bond-introducing enzyme, across the Escherichia coli cytoplasmic membrane was studied with special reference to the effects of various mutations affecting translocation factors. It was noted that both the internalized precursor retaining the signal peptide and the periplasmic mature product fold rapidly into a protease-resistant structure and they exhibited anomalies in sodium dodecyl sulfate-polyacrylamide gel electrophoresis in that the former migrated faster than the latter. The precursor, once accumulated, was not exported posttranslationally. DsbA export depended on the SecY translocon, the SecA ATPase, and Ffh (signal recognition particle), but not on SecB. SecY mutations, such as secY39 and secY205, that severely impair translocation of a number of secretory substrates by interfering with SecA actions only insignificantly impaired the DsbA export. In contrast, secY125, affecting a periplasmic domain and impairing a late step of translocation, exerted strong export inhibition of both classes of proteins. These results suggest that DsbA uses not only the signal recognition particle targeting pathway but also a special route of translocation through the translocon, which is hence suggested to actively discriminate pre-proteins.
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Registered trials
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