{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T02:44:19Z","timestamp":1790909059024,"version":"4.1.0"},"reference-count":54,"publisher":"National Academy of Sciences","issue":"51","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2009,12,22]]},"abstract":"<jats:p>\n                    Hydrogenosomes and mitosomes are mitochondrion-related organelles in anaerobic\/microaerophilic eukaryotes with highly reduced and divergent functions. The full diversity of their content and function, however, has not been fully determined. To understand the central role of mitosomes in\n                    <jats:italic>Entamoeba histolytica<\/jats:italic>\n                    , a parasitic protozoon that causes amoebic dysentery and liver abscesses, we examined the proteomic profile of purified mitosomes. Using 2 discontinuous Percoll gradient centrifugation and MS analysis, we identified 95 putative mitosomal proteins. Immunofluorescence assay showed that 3 proteins involved in sulfate activation, ATP sulfurylase, APS kinase, and inorganic pyrophosphatase, as well as sodium\/sulfate symporter, involved in sulfate uptake, were compartmentalized to mitosomes. We have also provided biochemical evidence that activated sulfate derivatives, adenosine-5\u2032-phosphosulfate and 3\u2032-phosphoadenosine-5\u2032-phosphosulfate, were produced in mitosomes. Phylogenetic analysis showed that the aforementioned proteins and chaperones have distinct origins, suggesting the mosaic character of mitosomes in\n                    <jats:italic>E. histolytica<\/jats:italic>\n                    consisting of proteins derived from \u03b1-proteobacterial, \u03b4-proteobacterial, and ancestral eukaryotic origins. These results suggest that sulfate activation is the major function of mitosomes in\n                    <jats:italic>E. histolytica<\/jats:italic>\n                    and that\n                    <jats:italic>E. histolytica<\/jats:italic>\n                    mitosomes represent a unique mitochondrion-related organelle with remarkable diversity.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0907106106","type":"journal-article","created":{"date-parts":[[2009,12,8]],"date-time":"2009-12-08T00:32:56Z","timestamp":1260232376000},"page":"21731-21736","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":134,"title":["Mitosomes in\n                    <i>Entamoeba histolytica<\/i>\n                    contain a sulfate activation pathway"],"prefix":"10.1073","volume":"106","author":[{"given":"Fumika","family":"Mi-ichi","sequence":"first","affiliation":[{"name":"Department of Parasitology, National Institute of Infectious Diseases, 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