ArticleJournal of bacteriology1996
Influence of impaired chaperone or secretion function on SecB production in Escherichia coli.
Article in Journal of bacteriology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
7 citing papers in PubMed.
- The Sec System: Protein Export inEcoSal Plus · 2017Review
- Multitasking SecB chaperones in bacteria.Frontiers in microbiology · 2014Review
- Biogenesis of bacterial inner-membrane proteins.Cellular and molecular life sciences : CMLS · 2010Review
- The signal recognition particle pathway is required for virulence in Streptococcus pyogenes.Infection and immunity · 2008Article
- Trigger Factor can antagonize both SecB and DnaK/DnaJ chaperone functions in Escherichia coli.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- SecB is a bona fide generalized chaperone in Escherichia coli.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Protein targeting to the bacterial cytoplasmic membrane.Microbiology and molecular biology reviews : MMBR · 1999Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The efficient export of proteins through the cytoplasmic membrane of Escherichia coli requires chaperones to maintain protein precursors in a translocation-competent conformation. In addition to SecB, the major chaperone facilitating export of particular precursors, heat shock-induced chaperones DnaK-DnaJ and GroEL-GroES are also involved in this process. By use of secB'-lacZ gene fusions and immunoprecipitation experiments, SecB production was studied in E. coli strains containing conditional lethal mutations in chaperone or sec genes. While the loss of heat shock chaperones resulted in an increased production of SecB, mutations in sec genes showed only minor effects on SecB synthesis. Neither the plasmid-mediated overexpression of precursors of exoproteins nor the overexpression of secB altered the synthesis of SecB. These results suggest that under conditions where chaperones become depleted, E. coli responds by raising the expression of secB. These data confirm the supposed synergy of different chaperones involved in protein export.
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Registered trials
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