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However, the roles of chaperones during primary biogenesis in vivo can differ from the functions they play during in vitro refolding experiments. Here, we use limited proteolysis mass spectrometry (LiP-MS) to probe structural changes incurred by the\n                    <jats:italic>E. coli<\/jats:italic>\n                    proteome when two key chaperones, trigger factor and DnaKJ, are deleted. While knocking out DnaKJ induces pervasive structural perturbations across the soluble\n                    <jats:italic>E. coli<\/jats:italic>\n                    proteome, trigger factor deletion only impacts a small number of proteins\u2019 structures. Overall, proteins which cannot spontaneously refold (or require chaperones to refold in vitro) are\n                    <jats:italic>not<\/jats:italic>\n                    more likely to be dependent on chaperones to fold in vivo. We find that chaperone-nonrefolders (proteins that cannot refold even with chaperone assistance) do not generally require chaperones to fold in vivo, strengthening the view that chaperone-nonrefolders are obligate co-translational folders. Hence, for some\n                    <jats:italic>E. coli<\/jats:italic>\n                    proteins, the vectorial nature of co-translational folding is the most important \u201cchaperone\u201d.\n                  <\/jats:p>","DOI":"10.1038\/s44320-025-00166-6","type":"journal-article","created":{"date-parts":[[2025,10,28]],"date-time":"2025-10-28T11:29:11Z","timestamp":1761650951000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Chaperone dependency during biogenesis does not correlate with chaperone dependency during refolding"],"prefix":"10.1038","volume":"22","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2431-1917","authenticated-orcid":false,"given":"Divya","family":"Yadav","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5772-4710","authenticated-orcid":false,"given":"\u0130dil I","family":"Demiralp","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0003-2570-8638","authenticated-orcid":false,"given":"Mark","family":"Fakler","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2494-2193","authenticated-orcid":false,"given":"Stephen D","family":"Fried","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2025,10,28]]},"reference":[{"key":"166_CR1","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1016\/0003-2697(90)90104-H","volume":"189","author":"K Akimoto","year":"1990","unstructured":"Akimoto K, Shinmen Y, Sumida M, Asami S, Amachi T, Yoshizumi H, Saeki Y, Shimizu S, Yamada H (1990) Luminol chemiluminescence reaction catalyzed by a microbial peroxidase. 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