Genetic evidence that an endosymbiont-derived endoplasmic reticulum-associated protein degradation (ERAD) system functions in import of apicoplast proteins
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Agrawal, Swati; van Dooren, Giel; Beatty, Wandy L.; Striepen, Boris
Description
Most apicomplexan parasites harbor a relict chloroplast, the apicoplast, that is critical for their survival. Whereas the apicoplast maintains a small genome, the bulk of its proteins are nuclear encoded and imported into the organelle. Several models have been proposed to explain how proteins might cross the four membranes that surround the apicoplast; however, experimental data discriminating these models are largely missing. Here we present genetic evidence that apicoplast protein import...[Show more]
dc.contributor.author | Agrawal, Swati | |
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dc.contributor.author | van Dooren, Giel | |
dc.contributor.author | Beatty, Wandy L. | |
dc.contributor.author | Striepen, Boris | |
dc.date.accessioned | 2015-12-13T22:48:52Z | |
dc.identifier.issn | 0021-9258 | |
dc.identifier.uri | http://hdl.handle.net/1885/80262 | |
dc.description.abstract | Most apicomplexan parasites harbor a relict chloroplast, the apicoplast, that is critical for their survival. Whereas the apicoplast maintains a small genome, the bulk of its proteins are nuclear encoded and imported into the organelle. Several models have been proposed to explain how proteins might cross the four membranes that surround the apicoplast; however, experimental data discriminating these models are largely missing. Here we present genetic evidence that apicoplast protein import depends on elements derived from the ER-associated protein degradation (ERAD) system of the endosymbiont. We identified two sets of ERAD components in Toxoplasma gondii, one associated with the ER and cytoplasm and one localized to the membranes of the apicoplast. We engineered a conditional null mutant in apicoplast Der1, the putative pore of the apicoplast ERAD complex, and found that loss of Der1Ap results in loss of apicoplast protein import and subsequent death of the parasite. | |
dc.publisher | American Society for Biochemistry and Molecular Biology Inc | |
dc.source | Journal of Biological Chemistry | |
dc.subject | Keywords: Apicomplexan parasites; Endoplasmic reticulum; Endosymbiont; Experimental data; Null mutant; Parasite-; Protein degradation; Protein import; System functions; Toxoplasma gondii; Chlorophyll; Cytology; Degradation; Proteins; cell protein; protein Der1; unc | |
dc.title | Genetic evidence that an endosymbiont-derived endoplasmic reticulum-associated protein degradation (ERAD) system functions in import of apicoplast proteins | |
dc.type | Journal article | |
local.description.notes | Imported from ARIES | |
local.identifier.citationvolume | 284 | |
dc.date.issued | 2009 | |
local.identifier.absfor | 060104 - Cell Metabolism | |
local.identifier.ariespublication | f5625xPUB8546 | |
local.type.status | Published Version | |
local.contributor.affiliation | Agrawal, Swati, University of Georgia | |
local.contributor.affiliation | van Dooren, Giel, College of Medicine, Biology and Environment, ANU | |
local.contributor.affiliation | Beatty, Wandy L., University of Georgia | |
local.contributor.affiliation | Striepen, Boris, University of Georgia | |
local.description.embargo | 2037-12-31 | |
local.bibliographicCitation.issue | 48 | |
local.bibliographicCitation.startpage | 33683 | |
local.bibliographicCitation.lastpage | 33691 | |
local.identifier.doi | 10.1074/jbc.M109.044024 | |
local.identifier.absseo | 920109 - Infectious Diseases | |
dc.date.updated | 2016-02-24T09:42:51Z | |
local.identifier.scopusID | 2-s2.0-70450251981 | |
local.identifier.thomsonID | 000272028500072 | |
Collections | ANU Research Publications |
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