<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>10(2)</volume><submitter>Erives AJ</submitter><pubmed_abstract>The evolution of animals involved acquisition of an emergent gene repertoire for gastrulation. Whether loss of genes also co-evolved with this developmental reprogramming has not yet been addressed. Here, we identify twenty-four genetic functions that are retained in fungi and choanoflagellates but undetectable in animals. These lost genes encode: (i) sixteen distinct biosynthetic functions; (ii) the two ancestral eukaryotic ClpB disaggregases, Hsp78 and Hsp104, which function in the mitochondria and cytosol, respectively; and (iii) six other assorted functions. We present computational and experimental data that are consistent with a joint function for the differentially localized ClpB disaggregases, and with the possibility of a shared client/chaperone relationship between the mitochondr</pubmed_abstract><journal>PloS one</journal><pagination>e0117192</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4339202</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Metabolic and chaperone gene loss marks the origin of animals: evidence for Hsp104 and Hsp78 chaperones sharing mitochondrial enzymes as clients.</pubmed_title><pmcid>PMC4339202</pmcid><pubmed_authors>Erives AJ</pubmed_authors><pubmed_authors>Fassler JS</pubmed_authors></additional><is_claimable>false</is_claimable><name>Metabolic and chaperone gene loss marks the origin of animals: evidence for Hsp104 and Hsp78 chaperones sharing mitochondrial enzymes as clients.</name><description>The evolution of animals involved acquisition of an emergent gene repertoire for gastrulation. Whether loss of genes also co-evolved with this developmental reprogramming has not yet been addressed. Here, we identify twenty-four genetic functions that are retained in fungi and choanoflagellates but undetectable in animals. These lost genes encode: (i) sixteen distinct biosynthetic functions; (ii) the two ancestral eukaryotic ClpB disaggregases, Hsp78 and Hsp104, which function in the mitochondria and cytosol, respectively; and (iii) six other assorted functions. We present computational and experimental data that are consistent with a joint function for the differentially localized ClpB disaggregases, and with the possibility of a shared client/chaperone relationship between the mitochondr</description><dates><release>2015-01-01T00:00:00Z</release><publication>2015</publication><modification>2026-04-13T14:07:22.995Z</modification><creation>2019-03-26T23:30:24Z</creation></dates><accession>S-EPMC4339202</accession><cross_references><pubmed>25710177</pubmed><doi>10.1371/journal.pone.0117192</doi></cross_references></HashMap>