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- W2843647573 abstract "Peptidoglycan biosynthesis is a dynamic and well-controlled pathway. The molecular assembly of PG and the regulatory pathways ensuring its maintenance are still not well understood. Here we studied the newly discovered Escherichia coli factor ElyC, which is important for PG biosynthesis at low temperatures. We revealed an important protein-folding defect in the Δ elyC mutant and showed that overproduction of the periplasmic chaperone DsbG or Spy was sufficient to correct the protein-folding defect and restore PG biosynthesis. These results show that the PG defect in the absence of ElyC is caused, at least in part, by a protein-folding problem in the cell envelope. Furthermore, we showed, for the first time, that the periplasmic protein DsbG has chaperone activity in vivo ." @default.
- W2843647573 created "2018-07-19" @default.
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- W2843647573 date "2018-10-01" @default.
- W2843647573 modified "2023-10-02" @default.
- W2843647573 title "The Chaperone Activities of DsbG and Spy Restore Peptidoglycan Biosynthesis in the <i>elyC</i> Mutant by Preventing Envelope Protein Aggregation" @default.
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- W2843647573 doi "https://doi.org/10.1128/jb.00245-18" @default.
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