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The molecular assembly of PG and the regulatory pathways ensuring its maintenance are still not well understood. Here we studied the newly discovered\n            <jats:named-content content-type=\"genus-species\">Escherichia coli<\/jats:named-content>\n            factor ElyC, which is important for PG biosynthesis at low temperatures. We revealed an important protein-folding defect in the \u0394\n            <jats:italic>elyC<\/jats:italic>\n            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\n            <jats:italic>in vivo<\/jats:italic>\n            .\n          <\/jats:p>","DOI":"10.1128\/jb.00245-18","type":"journal-article","created":{"date-parts":[[2018,7,12]],"date-time":"2018-07-12T10:06:11Z","timestamp":1531389971000},"update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":8,"title":["The Chaperone Activities of DsbG and Spy Restore Peptidoglycan Biosynthesis in the\n            <i>elyC<\/i>\n            Mutant by Preventing Envelope Protein Aggregation"],"prefix":"10.1128","volume":"200","author":[{"given":"Im\u00e8ne","family":"Kouidmi","sequence":"first","affiliation":[{"name":"D\u00e9partement de Microbiologie, Infectiologie et Immunologie, Universit\u00e9 de Montr\u00e9al, Montreal, Quebec, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Laura","family":"Alvarez","sequence":"additional","affiliation":[{"name":"Laboratory for Molecular Infection Medicine Sweden, Department of Molecular Biology, Ume\u00e5 Center for Microbial Research, Ume\u00e5, Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jean Fran\u00e7ois","family":"Collet","sequence":"additional","affiliation":[{"name":"De Duve Institute, Universit\u00e9 Catholique de Louvain, Brussels, Belgium"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Felipe","family":"Cava","sequence":"additional","affiliation":[{"name":"Laboratory for Molecular Infection Medicine Sweden, Department of Molecular Biology, Ume\u00e5 Center for Microbial Research, Ume\u00e5, Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Catherine","family":"Paradis-Bleau","sequence":"additional","affiliation":[{"name":"D\u00e9partement de Microbiologie, Infectiologie et Immunologie, Universit\u00e9 de Montr\u00e9al, Montreal, Quebec, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1101\/cshperspect.a000414"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.tim.2010.06.005"},{"key":"e_1_3_3_4_2","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1111\/j.1432-1033.1970.tb00936.x","article-title":"The covalent murein-lipoprotein structure of the Escherichia coli cell wall. 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