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In bacteria, Hsp70 (DnaK) operates with the J\u2010domain cochaperone DnaJ and the nucleotide exchange factor (NEF) GrpE, which accelerates ADP release and ATP rebinding. Many simple prokaryotes encode a single canonical DnaK, but more complex bacteria often harbor additional DnaK\u2010derived paralogues with modified, truncated, or missing domains required for substrate and DnaJ binding, raising questions about their functions and possible roles in proteostasis. A suggestive parallel comes from eukaryogenesis, when a gene duplication of an ancestral Hsp70 gave rise to Hsp110. Hsp110s have largely abandoned direct DnaJ, GrpE, and substrate binding; yet, through the reversible formation of NBD\u2010mediated Hsp70\u2013Hsp110 heterodimers, they act as potent NEFs that enhance Hsp70\u2010driven disaggregation of compact protein aggregates. By analogy, we propose that NBD\u2010containing DnaK paralogues in prokaryotes may likewise function as dedicated DnaK cochaperones, tuned to boost protein disaggregation and repair and specialized for the specific lifestyles and associated stressors of these organisms.<\/jats:p>","DOI":"10.1111\/febs.70535","type":"journal-article","created":{"date-parts":[[2026,4,15]],"date-time":"2026-04-15T03:45:01Z","timestamp":1776224701000},"page":"5541-5557","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Hsp70 diversification and repurposing across the tree of life: Lessons from the evolutionary and mechanistic trajectory of the Hsp70\u2013Hsp110 chaperone system"],"prefix":"10.1111","volume":"293","author":[{"given":"Pierre","family":"Goloubinoff","sequence":"first","affiliation":[{"name":"Department of Plant Molecular Biology, Faculty of Biology and Medicine University of Lausanne  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