Autophagy-related Atg8 localizes to the apicoplast of the human malaria parasite Plasmodium falciparum
Autophagy is a membrane-mediated degradation process, which is governed by sequential functions of Atg proteins. Although Atg proteins are highly conserved in eukaryotes, protozoa possess only a partial set of Atg proteins. Nonetheless, almost all protozoa have the complete factors belonging to the...
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| creator | Kitamura, Kei Kishi-Itakura, Chieko Tsuboi, Takafumi Sato, Shigeharu Kita, Kiyoshi Ohta, Nobuo Mizushima, Noboru |
| description | Autophagy is a membrane-mediated degradation process, which is governed by sequential functions of Atg proteins. Although Atg proteins are highly conserved in eukaryotes, protozoa possess only a partial set of Atg proteins. Nonetheless, almost all protozoa have the complete factors belonging to the Atg8 conjugation system, namely, Atg3, Atg4, Atg7, and Atg8. Here, we report the biochemical properties and subcellular localization of the Atg8 protein of the human malaria parasite Plasmodium falciparum (PfAtg8). PfAtg8 is expressed during intra-erythrocytic development and associates with membranes likely as a lipid-conjugated form. Fluorescence microscopy and immunoelectron microscopy show that PfAtg8 localizes to the apicoplast, a four membrane-bound non-photosynthetic plastid. Autophagosome-like structures are not observed in the erythrocytic stages. These data suggest that, although Plasmodium parasites have lost most Atg proteins during evolution, they use the Atg8 conjugation system for the unique organelle, the apicoplast. |
| doi_str_mv | 10.1371/journal.pone.0042977 |
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Although Atg proteins are highly conserved in eukaryotes, protozoa possess only a partial set of Atg proteins. Nonetheless, almost all protozoa have the complete factors belonging to the Atg8 conjugation system, namely, Atg3, Atg4, Atg7, and Atg8. Here, we report the biochemical properties and subcellular localization of the Atg8 protein of the human malaria parasite Plasmodium falciparum (PfAtg8). PfAtg8 is expressed during intra-erythrocytic development and associates with membranes likely as a lipid-conjugated form. Fluorescence microscopy and immunoelectron microscopy show that PfAtg8 localizes to the apicoplast, a four membrane-bound non-photosynthetic plastid. Autophagosome-like structures are not observed in the erythrocytic stages. These data suggest that, although Plasmodium parasites have lost most Atg proteins during evolution, they use the Atg8 conjugation system for the unique organelle, the apicoplast.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0042977</identifier><identifier>PMID: 22900071</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino Acid Sequence ; Antigens ; Antimalarials - pharmacology ; Autophagy ; Biology ; Cell death ; Cell Membrane - metabolism ; Chloroquine - pharmacology ; Conjugation ; Endoplasmic reticulum ; Enzymes ; Erythrocytes ; Erythrocytes - metabolism ; Erythrocytes - parasitology ; Eukaryotes ; Fluorescence ; Fluorescence microscopy ; Genomes ; Humans ; Immunoelectron microscopy ; Localization ; Malaria ; Medicine ; Membranes ; Microscopy ; Molecular Sequence Data ; Parasites ; Parasitology ; Phagocytosis ; Photosynthesis ; Physiology ; Plasmodium ; Plasmodium falciparum ; Plasmodium falciparum - genetics ; Plasmodium falciparum - metabolism ; Plasmodium falciparum - ultrastructure ; Plastids - metabolism ; Protein Transport - drug effects ; Proteins ; Protozoa ; Protozoan Proteins - chemistry ; Protozoan Proteins - genetics ; Protozoan Proteins - metabolism ; Saccharomyces cerevisiae ; Sequence Alignment ; Stem cells ; Toxoplasma gondii ; Vector-borne diseases</subject><ispartof>PloS one, 2012-08, Vol.7 (8), p.e42977-e42977</ispartof><rights>COPYRIGHT 2012 Public Library of Science</rights><rights>Kitamura et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2012 Kitamura et al 2012 Kitamura et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c758t-f109282f9a478520e72520df5d16b08d5eb489c5bc91e2346e66409219bd6b603</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3416769/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3416769/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79342,79343</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22900071$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kitamura, Kei</creatorcontrib><creatorcontrib>Kishi-Itakura, Chieko</creatorcontrib><creatorcontrib>Tsuboi, Takafumi</creatorcontrib><creatorcontrib>Sato, Shigeharu</creatorcontrib><creatorcontrib>Kita, Kiyoshi</creatorcontrib><creatorcontrib>Ohta, Nobuo</creatorcontrib><creatorcontrib>Mizushima, Noboru</creatorcontrib><title>Autophagy-related Atg8 localizes to the apicoplast of the human malaria parasite Plasmodium falciparum</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Autophagy is a membrane-mediated degradation process, which is governed by sequential functions of Atg proteins. Although Atg proteins are highly conserved in eukaryotes, protozoa possess only a partial set of Atg proteins. Nonetheless, almost all protozoa have the complete factors belonging to the Atg8 conjugation system, namely, Atg3, Atg4, Atg7, and Atg8. Here, we report the biochemical properties and subcellular localization of the Atg8 protein of the human malaria parasite Plasmodium falciparum (PfAtg8). PfAtg8 is expressed during intra-erythrocytic development and associates with membranes likely as a lipid-conjugated form. Fluorescence microscopy and immunoelectron microscopy show that PfAtg8 localizes to the apicoplast, a four membrane-bound non-photosynthetic plastid. Autophagosome-like structures are not observed in the erythrocytic stages. These data suggest that, although Plasmodium parasites have lost most Atg proteins during evolution, they use the Atg8 conjugation system for the unique organelle, the apicoplast.</description><subject>Amino Acid Sequence</subject><subject>Antigens</subject><subject>Antimalarials - pharmacology</subject><subject>Autophagy</subject><subject>Biology</subject><subject>Cell death</subject><subject>Cell Membrane - metabolism</subject><subject>Chloroquine - pharmacology</subject><subject>Conjugation</subject><subject>Endoplasmic reticulum</subject><subject>Enzymes</subject><subject>Erythrocytes</subject><subject>Erythrocytes - metabolism</subject><subject>Erythrocytes - parasitology</subject><subject>Eukaryotes</subject><subject>Fluorescence</subject><subject>Fluorescence microscopy</subject><subject>Genomes</subject><subject>Humans</subject><subject>Immunoelectron microscopy</subject><subject>Localization</subject><subject>Malaria</subject><subject>Medicine</subject><subject>Membranes</subject><subject>Microscopy</subject><subject>Molecular Sequence Data</subject><subject>Parasites</subject><subject>Parasitology</subject><subject>Phagocytosis</subject><subject>Photosynthesis</subject><subject>Physiology</subject><subject>Plasmodium</subject><subject>Plasmodium falciparum</subject><subject>Plasmodium falciparum - 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Although Atg proteins are highly conserved in eukaryotes, protozoa possess only a partial set of Atg proteins. Nonetheless, almost all protozoa have the complete factors belonging to the Atg8 conjugation system, namely, Atg3, Atg4, Atg7, and Atg8. Here, we report the biochemical properties and subcellular localization of the Atg8 protein of the human malaria parasite Plasmodium falciparum (PfAtg8). PfAtg8 is expressed during intra-erythrocytic development and associates with membranes likely as a lipid-conjugated form. Fluorescence microscopy and immunoelectron microscopy show that PfAtg8 localizes to the apicoplast, a four membrane-bound non-photosynthetic plastid. Autophagosome-like structures are not observed in the erythrocytic stages. These data suggest that, although Plasmodium parasites have lost most Atg proteins during evolution, they use the Atg8 conjugation system for the unique organelle, the apicoplast.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>22900071</pmid><doi>10.1371/journal.pone.0042977</doi><tpages>e42977</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Antigens Antimalarials - pharmacology Autophagy Biology Cell death Cell Membrane - metabolism Chloroquine - pharmacology Conjugation Endoplasmic reticulum Enzymes Erythrocytes Erythrocytes - metabolism Erythrocytes - parasitology Eukaryotes Fluorescence Fluorescence microscopy Genomes Humans Immunoelectron microscopy Localization Malaria Medicine Membranes Microscopy Molecular Sequence Data Parasites Parasitology Phagocytosis Photosynthesis Physiology Plasmodium Plasmodium falciparum Plasmodium falciparum - genetics Plasmodium falciparum - metabolism Plasmodium falciparum - ultrastructure Plastids - metabolism Protein Transport - drug effects Proteins Protozoa Protozoan Proteins - chemistry Protozoan Proteins - genetics Protozoan Proteins - metabolism Saccharomyces cerevisiae Sequence Alignment Stem cells Toxoplasma gondii Vector-borne diseases |
| title | Autophagy-related Atg8 localizes to the apicoplast of the human malaria parasite Plasmodium falciparum |
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