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Eukaryotic heteromeric enzymes involved in polyprenyl chain elongation consist of a highly conserved catalytic\n                    <jats:italic>cis<\/jats:italic>\n                    \u2010prenyltransferase subunit (CPT\u2010CS) and a less conserved CPT\u2010accessory subunit (CPT\u2010AS). Here, we present the first experimental evidence that dolichol biosynthesis in\n                    <jats:italic>Paramecium tetraurelia<\/jats:italic>\n                    is mediated by a heteromeric CPT complex. Using a multidisciplinary experimental approach, we identified two highly homologous catalytic CPT subunits, CPT1a and CPT1b, which exhibit high sequence similarity to other eukaryotic CPTs, along with a unique CPT\u2010AS, named POC1 (partner of CPT1), which is a structural and functional relative of the human dehydrodolichyl diphosphate synthase complex subunit NUS1 (also known as NgBR) and yeast Nus1 CPT\u2010AS. Despite low sequence similarity to other CPT\u2010ASs, it retained a well\u2010preserved C\u2010terminal substrate\u2010binding domain characteristic of its eukaryotic and prokaryotic counterparts. The loss of POC1 or CPT1a, but not CPT1b, results in a deficit in dolichol production, leading to a significant reduction in glycoprotein content and, ultimately, to the\n                    <jats:italic>P.\u2009tetraurelia<\/jats:italic>\n                    cell death. In a heterologous yeast system, both CPTs in complex with POC1 synthesized polyprenyl chains. The identification of a POC1 protein so distinct from other CPT\u2010ASs may spark further efforts to uncover CPT\u2010AS proteins in pathogenic protozoa, which have so far eluded detection despite phylogenetic evidences that CPT of\n                    <jats:italic>Apicomplexa<\/jats:italic>\n                    and\n                    <jats:italic>Trichomonas sp<\/jats:italic>\n                    . are heteromeric enzymes. Given their substantial sequence divergence from human NgBR and its animal orthologues, these protozoan CPT\u2010ASs could represent highly specific targets for antiparasitic therapies.\n                  <\/jats:p>","DOI":"10.1111\/febs.70237","type":"journal-article","created":{"date-parts":[[2025,8,23]],"date-time":"2025-08-23T06:52:03Z","timestamp":1755931923000},"page":"1681-1707","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Evolutionary divergence and functional insights into the heteromeric\n                    <i>cis<\/i>\n                    \u2010prenyltransferase of\n                    <i>Paramecium tetraurelia<\/i>"],"prefix":"10.1111","volume":"293","author":[{"given":"Agnieszka","family":"Onysk","sequence":"first","affiliation":[{"name":"Institute of Biochemistry and Biophysics Polish Academy of Sciences  Warsaw 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