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Cells must match the protein synthesis rate to the protein folding capacity to avoid the accumulation of unfolded proteins that can form toxic aggregates. The Hsp70 chaperone DnaK binds to ribosomes and decreases protein synthesis in the bacterial pathogen\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>Salmonella enterica<\/jats:italic>\n                    <\/jats:styled-content>\n                    serovar Typhimurium when facing cytoplasmic Mg\n                    <jats:sup>2+<\/jats:sup>\n                    starvation, an infection\u2010relevant stress that disrupts proteostasis. DnaK decreases protein synthesis independently of J\u2010domain cochaperones and nucleotide exchange factor GrpE even though J\u2010domain cochaperones and GrpE are required for DnaK's canonical role in protein folding and refolding. DnaK's activity contrasts with that exhibited by the bacteria\u2010specific chaperone trigger factor, which associates with ribosomes and carries out cotranslational protein folding in Mg\n                    <jats:sup>2+<\/jats:sup>\n                    \u2010abundant conditions. Under infection\u2010relevant conditions, the master regulator of\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>S. typhimurium<\/jats:italic>\n                    <\/jats:styled-content>\n                    virulence and Mg\n                    <jats:sup>2+<\/jats:sup>\n                    homeostasis PhoP promotes the expression of DnaK, but not of J\u2010domain cochaperones, GrpE, or trigger factor, suggesting that the differential expression of chaperones and cochaperones furthers\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>S. typhimurium<\/jats:italic>\n                    <\/jats:styled-content>\n                    pathogenesis. Hsp70 chaperones also associate with ribosomes in eukaryotic cells but instead promote protein synthesis, the opposite effect that DnaK binding to ribosomes has in bacteria. Thus, Hsp70 chaperone activity differs across growth conditions and among organisms.\n                  <\/jats:p>","DOI":"10.1111\/mmi.70034","type":"journal-article","created":{"date-parts":[[2025,11,4]],"date-time":"2025-11-04T18:57:49Z","timestamp":1762282669000},"page":"13-26","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["How Pathogens Maintain Proteostasis During Infection"],"prefix":"10.1111","volume":"125","author":[{"given":"Carissa","family":"Chan","sequence":"first","affiliation":[{"name":"Department of Microbial Pathogenesis Yale School of Medicine  New Haven Connecticut USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6860-7691","authenticated-orcid":false,"given":"Eduardo A.","family":"Groisman","sequence":"additional","affiliation":[{"name":"Department of Microbial Pathogenesis Yale School of Medicine  New Haven Connecticut USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2025,11,4]]},"reference":[{"key":"e_1_2_13_2_1","doi-asserted-by":"publisher","DOI":"10.1128\/JB.01896-14"},{"key":"e_1_2_13_3_1","doi-asserted-by":"publisher","DOI":"10.1128\/JB.188.7.2715-2720.2006"},{"key":"e_1_2_13_4_1","doi-asserted-by":"publisher","DOI":"10.1128\/JB.01544-12"},{"issue":"18","key":"e_1_2_13_5_1","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1128\/JB.00212-18","article-title":"Magnesium Suppresses Defects in the Formation of 70S Ribosomes as Well as in Sporulation Caused by Lack of Several Individual Ribosomal Proteins","volume":"200","author":"Akanuma G.","year":"2018","journal-title":"Journal of Bacteriology"},{"volume-title":"Molecular Biology of the Cell","year":"2022","author":"Alberts B.","key":"e_1_2_13_6_1"},{"key":"e_1_2_13_7_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2011.07804.x"},{"key":"e_1_2_13_8_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.tibs.2006.10.006"},{"key":"e_1_2_13_9_1","doi-asserted-by":"publisher","DOI":"10.1128\/JB.183.19.5482-5490.2001"},{"issue":"6","key":"e_1_2_13_10_1","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1128\/mBio.01170-17","article-title":"Identification of Fitness Determinants During Energy\u2010Limited Growth Arrest in \n                     Pseudomonas aeruginosa","volume":"8","author":"Basta D. 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