Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.biochi.2006.05.021
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dc.titleA relevant in vitro eukaryotic live-cell system for the evaluation of plasmodial protein localization
dc.contributor.authorChan, M.
dc.contributor.authorTan, D.S.H.
dc.contributor.authorWong, S.-H.
dc.contributor.authorSim, T.-S.
dc.date.accessioned2011-07-26T06:53:54Z
dc.date.available2011-07-26T06:53:54Z
dc.date.issued2006
dc.identifier.citationChan, M., Tan, D.S.H., Wong, S.-H., Sim, T.-S. (2006). A relevant in vitro eukaryotic live-cell system for the evaluation of plasmodial protein localization. Biochimie 88 (10) : 1367-1375. ScholarBank@NUS Repository. https://doi.org/10.1016/j.biochi.2006.05.021
dc.identifier.issn03009084
dc.identifier.issn61831638
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/24738
dc.description.abstractUnderstanding the functional genomics and proteomics of plasmodia underpins the development of new approaches to antimalarial chemotherapy. Although genome databanks (e.g. PlasmoDB) and biocomputing tools (e.g. PlasMit, PlasmoAP, PATS) are useful in providing a global albeit predictive view of the myriad of about 5000 genes, only 40% are annotated, with few cases of endorsed subcellular localizations of the corresponding proteins in animal models. Progress in plasmodial protein trafficking has been hampered by the lack of a simple yet reliable method for studying subcellular localization of plasmodial proteins. In this study, we have used a combination of fluorescent markers, organelle-specific probes, phase contrast microscopy, and confocal microscopy to locate a selection of signal peptides from 10 plasmodial proteins in CHO-K1 cells. These eukaryotic cells serve as an in vitro living system for studying the cellular destinations of four mitochondrial-targeted TCA cycle proteins (citrate synthase, CS; isocitrate dehydrogenase, ICDH; branched chain α-keto-acid dehydrogenase E1α subunit, BCKDH; succinate dehydrogenase flavoprotein-subunit, SDH), two nuclear-targeted proteins (histone deacetylase, HDAC; RNA polymerase, RPOL), two apicoplast-targeted proteins (pyruvate kinase 2, PK2; glutamate dehydrogenase, GDH), and two cytoplasmic resident proteins (malate dehydrogenase, MDH; glycerol kinase, GK). The respective localizations of these malarial proteins have complied with the selected molecular targets, viz. mitochondrial, nuclear and cytoplasmic. Interestingly, MDH that is widely known to be resident in eukaryotic mitochondria was found to be cytoplasmic, probably due to the absence of molecular target sequences. Since the localization of plasmodial proteins is central to the authentication of their pathophysiological roles, this experimental system will serve as a useful a priori approach. © 2006 Elsevier Masson SAS. All rights reserved.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.biochi.2006.05.021
dc.sourceScopus
dc.subjectGreen fluorescent protein
dc.subjectHeterologous expression
dc.subjectLocalization
dc.subjectMalaria
dc.subjectPlasmodium falciparum
dc.typeArticle
dc.contributor.departmentMICROBIOLOGY
dc.description.doi10.1016/j.biochi.2006.05.021
dc.description.sourcetitleBiochimie
dc.description.volume88
dc.description.issue10
dc.description.page1367-1375
dc.identifier.isiut000242460000006
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