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dc.contributor.authorMullin, KA
dc.contributor.authorLim, L
dc.contributor.authorRalph, SA
dc.contributor.authorSpurck, TP
dc.contributor.authorHandman, E
dc.contributor.authorMcFadden, GI
dc.date.available2014-05-21T19:35:25Z
dc.date.issued2006-06-20
dc.identifierpii: 0602293103
dc.identifier.citationMullin, K. A., Lim, L., Ralph, S. A., Spurck, T. P., Handman, E. & McFadden, G. I. (2006). Membrane transporters in the relict plastid of malaria parasites. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 103 (25), pp.9572-9577. https://doi.org/10.1073/pnas.0602293103.
dc.identifier.issn0027-8424
dc.identifier.urihttp://hdl.handle.net/11343/26502
dc.descriptionC1 - Journal Articles Refereed
dc.description.abstractMalaria parasites contain a nonphotosynthetic plastid homologous to chloroplasts of plants. The parasite plastid synthesizes fatty acids, heme, iron sulfur clusters and isoprenoid precursors and is indispensable, making it an attractive target for antiparasite drugs. How parasite plastid biosynthetic pathways are fuelled in the absence of photosynthetic capture of energy and carbon was not clear. Here, we describe a pair of parasite transporter proteins, PfiTPT and PfoTPT, that are homologues of plant chloroplast innermost membrane transporters responsible for moving phosphorylated C3, C5, and C6 compounds across the plant chloroplast envelope. PfiTPT is shown to be localized in the innermost membrane of the parasite plastid courtesy of a cleavable N-terminal targeting sequence. PfoTPT lacks such a targeting sequence, but is shown to localize in the outermost parasite plastid membrane with its termini projecting into the cytosol. We have identified these membrane proteins in the parasite plastid and determined membrane orientation for PfoTPT. PfiTPT and PfoTPT are proposed to act in tandem to transport phosphorylated C3 compounds from the parasite cytosol into the plastid. Thus, the transporters could shunt glycolytic derivatives of glucose scavenged from the host into the plastid providing carbon, reducing equivalents and ATP to power the organelle.
dc.formatapplication/pdf
dc.languageEnglish
dc.publisherNATL ACAD SCIENCES
dc.subjectProtein Targeting and Signal Transduction; Infectious Diseases
dc.titleMembrane transporters in the relict plastid of malaria parasites
dc.typeJournal Article
dc.identifier.doi10.1073/pnas.0602293103
melbourne.peerreviewPeer Reviewed
melbourne.affiliationThe University of Melbourne
melbourne.affiliation.departmentBotany
melbourne.source.titlePROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
melbourne.source.volume103
melbourne.source.issue25
melbourne.source.pages9572-9577
dc.research.coderfcd270103
dc.research.codeseo1998730101
melbourne.publicationid56508
melbourne.elementsid280222
melbourne.openaccess.pmchttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC1480448
melbourne.contributor.authorMcFadden, Geoffrey
melbourne.contributor.authorMULLIN, KYLIE
melbourne.contributor.authorSPURCK, TIMOTHY
melbourne.contributor.authorRalph, Stuart
melbourne.contributor.authorLIM, LITING
dc.identifier.eissn1091-6490
melbourne.accessrightsAccess this item via the Open Access location


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