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dc.contributor.authorvan Dooren, GG
dc.contributor.authorSu, V
dc.contributor.authorD'Ombrain, C
dc.contributor.authorMcFadden, GI
dc.date.available2014-05-21T19:40:38Z
dc.date.issued2002-06-28
dc.identifierpii: M201748200
dc.identifier.citationvan Dooren, G. G., Su, V., D'Ombrain, C. & McFadden, G. I. (2002). Processing of an apicoplast leader sequence in Plasmodium falciparum and the identification of a putative leader cleavage enzyme. JOURNAL OF BIOLOGICAL CHEMISTRY, 277 (26), pp.23612-23619. https://doi.org/10.1074/jbc.M201748200.
dc.identifier.issn0021-9258
dc.identifier.urihttp://hdl.handle.net/11343/26619
dc.descriptionC1 - Journal Articles Refereed
dc.description.abstractThe plastid (apicoplast) of the malaria-causing parasite Plasmodium falciparum was derived via a secondary endosymbiotic process. As in other secondary endosymbionts, numerous genes for apicoplast proteins are located in the nucleus, and the encoded proteins are targeted to the organelle courtesy of a bipartite N-terminal extension. The first part of this leader sequence is a signal peptide that targets proteins to the secretory pathway. The second, so-called transit peptide region is required to direct proteins from the secretory pathway across the multiple membranes surrounding the apicoplast. In this paper we perform a pulse-chase experiment and N-terminal sequencing to show that the transit peptide of an apicoplast-targeted protein is cleaved, presumably upon import of the protein into the apicoplast. We identify a gene whose product likely performs this cleavage reaction, namely a stromal-processing peptidase (SPP) homologue. In plants SPP cleaves the transit peptides of plastid-targeted proteins. The P. falciparum SPP homologue contains a bipartite N-terminal apicoplast-targeting leader. Interestingly, it shares this leader sequence with a Delta-aminolevulinic acid dehydratase homologue via an alternative splicing event.
dc.formatapplication/pdf
dc.languageEnglish
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
dc.subjectInfectious Agents; Infectious Diseases
dc.titleProcessing of an apicoplast leader sequence in Plasmodium falciparum and the identification of a putative leader cleavage enzyme
dc.typeJournal Article
dc.identifier.doi10.1074/jbc.M201748200
melbourne.peerreviewPeer Reviewed
melbourne.affiliationThe University of Melbourne
melbourne.affiliation.departmentBotany
melbourne.source.titleJOURNAL OF BIOLOGICAL CHEMISTRY
melbourne.source.volume277
melbourne.source.issue26
melbourne.source.pages23612-23619
dc.research.coderfcd270304
dc.research.codeseo1998730101
melbourne.publicationid9732
melbourne.elementsid252136
melbourne.contributor.authorVAN DOOREN, GIEL GODEFRIDUS
melbourne.contributor.authorMollard, Vanessa
melbourne.contributor.authorD'OMBRAIN, MARTHE
melbourne.contributor.authorMcFadden, Geoffrey
dc.identifier.eissn1083-351X
melbourne.accessrightsThis item is currently not available from this repository


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