{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,8]],"date-time":"2026-06-08T14:54:55Z","timestamp":1780930495635,"version":"3.54.1"},"reference-count":56,"publisher":"American Society for Microbiology","issue":"2","license":[{"start":{"date-parts":[[2006,2,1]],"date-time":"2006-02-01T00:00:00Z","timestamp":1138752000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Eukaryot Cell"],"published-print":{"date-parts":[[2006,2]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            J-domain (DnaJ) proteins, of the Hsp40 family, are essential cofactors of their cognate Hsp70 chaperones, besides acting as independent chaperones. In the present study, we have demonstrated the presence of Mdj1, a mitochondrial DnaJ member, not only in the mitochondria, where it is apparently sorted, but also in the cell wall of\n            <jats:italic>Paracoccidioides brasiliensis<\/jats:italic>\n            , a thermodimorphic pathogenic fungus. The molecule (PbMdj1) was localized to fungal yeast cells using both confocal and electron microscopy and also flow cytometry. The anti-recombinant PbMdj1 antibodies used in the reactions specifically recognized a single 55-kDa mitochondrial and cell wall (alkaline \u03b2-mercaptoethanol extract) component, compatible with the predicted size of the protein devoid of its matrix peptide-targeting signal. Labeling was abundant throughout the cell wall and especially in the budding regions; however, anti-PbMdj1 did not affect fungal growth in the concentrations tested in vitro, possibly due to the poor access of the antibodies to their target in growing cells. Labeled mitochondria stood preferentially close to the plasma membrane, and gold particles were detected in the thin space between them, toward the cell surface. We show that Mdj1 and the mitochondrial proteinase Lon homologues are heat shock proteins in\n            <jats:italic>P. brasiliensis<\/jats:italic>\n            and that their gene organizations are conserved among thermodimorphic fungi and\n            <jats:italic>Aspergillus<\/jats:italic>\n            , where the genes are adjacent and have a common 5\u2032 region. This is the first time a DnaJ member has been observed on the cell surface, where its function is speculative.\n          <\/jats:p>","DOI":"10.1128\/ec.5.2.379-390.2006","type":"journal-article","created":{"date-parts":[[2006,2,8]],"date-time":"2006-02-08T19:18:30Z","timestamp":1139426310000},"page":"379-390","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":29,"title":["The Pb\n            <i>MDJ1<\/i>\n            Gene Belongs to a Conserved\n            <i>MDJ1\/LON<\/i>\n            Locus in Thermodimorphic Pathogenic Fungi and Encodes a Heat Shock Protein That Localizes to both the Mitochondria and Cell Wall of\n            <i>Paracoccidioides brasiliensis<\/i>"],"prefix":"10.1128","volume":"5","author":[{"given":"Wagner L.","family":"Batista","sequence":"first","affiliation":[{"name":"Department of Microbiology, Immunology and Parasitology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alisson L.","family":"Matsuo","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Immunology and Parasitology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luciane","family":"Ganiko","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Immunology and Parasitology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ta\u0302nia F.","family":"Barros","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Immunology and Parasitology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thiago R.","family":"Veiga","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Immunology and Parasitology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Edna","family":"Freymu\u0308ller","sequence":"additional","affiliation":[{"name":"Center of Electron Microscopy, Federal University of Sa\u0303o Paulo, Rua Botucatu 862, 04023-062 Sa\u0303o Paulo, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rosana","family":"Puccia","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Immunology and Parasitology"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1002\/pmic.200400952"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1002\/yea.745"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/JCM.38.9.3190-3193.2000"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.freeradbiomed.2004.11.017"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(76)90527-3"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.96.2.533-543.1968"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.100.2.1076-1082.1969"},{"key":"e_1_3_2_9_2","doi-asserted-by":"crossref","unstructured":"Carvalho K. 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