• Login
    View Item 
    •   Home
    • Office of Sponsored Research (OSR)
    • KAUST Funded Research
    • Publications Acknowledging KAUST Support
    • View Item
    •   Home
    • Office of Sponsored Research (OSR)
    • KAUST Funded Research
    • Publications Acknowledging KAUST Support
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of KAUSTCommunitiesIssue DateSubmit DateThis CollectionIssue DateSubmit Date

    My Account

    Login

    Quick Links

    Open Access PolicyORCID LibguidePlumX LibguideSubmit an Item

    Statistics

    Display statistics

    Plasmodium Apicoplast Gln-tRNA Gln Biosynthesis Utilizes a Unique GatAB Amidotransferase Essential for Erythrocytic Stage Parasites

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Type
    Article
    Authors
    Mailu, Boniface M.
    Li, Ling
    Arthur, Jen
    Nelson, Todd M.
    Ramasamy, Gowthaman
    Fritz-Wolf, Karin
    Becker, Katja
    Gardner, Malcolm J.
    KAUST Grant Number
    FIC/2010/09
    Date
    2015-08-28
    Online Publication Date
    2015-08-28
    Print Publication Date
    2015-12-04
    Permanent link to this record
    http://hdl.handle.net/10754/599201
    
    Metadata
    Show full item record
    Abstract
    © 2015 by The American Society for Biochemistry and Molecular Biology, Inc. The malaria parasite Plasmodium falciparum apicoplast indirect aminoacylation pathway utilizes a non-discriminating glutamyl-tRNA synthetase to synthesize Glu-tRNAGln and a glutaminyl-tRNA amidotransferase to convert Glu-tRNAGln to Gln-tRNAGln. Here, we show that Plasmodium falciparum and other apicomplexans possess a unique heterodimeric glutamyltRNA amidotransferase consisting of GatA and GatB subunits (GatAB). We localized the P. falciparum GatA and GatB subunits to the apicoplast in blood stage parasites and demonstrated that recombinant GatAB converts Glu-tRNAGln to Gln-tRNAGln in vitro. We demonstrate that the apicoplast GatAB-catalyzed reaction is essential to the parasite blood stages because we could not delete the Plasmodium berghei gene encoding GatA in blood stage parasites in vivo. A phylogenetic analysis placed the split between Plasmodium GatB, archaeal GatE, and bacterial GatB prior to the phylogenetic divide between bacteria and archaea. Moreover, Plasmodium GatA also appears to have emerged prior to the bacterial-archaeal phylogenetic divide. Thus, although GatAB is found in Plasmodium, it emerged prior to the phylogenetic separation of archaea and bacteria.
    Citation
    Mailu BM, Li L, Arthur J, Nelson TM, Ramasamy G, et al. (2015) Plasmodium Apicoplast Gln-tRNA Gln Biosynthesis Utilizes a Unique GatAB Amidotransferase Essential for Erythrocytic Stage Parasites . J Biol Chem 290: 29629–29641. Available: http://dx.doi.org/10.1074/jbc.m115.655100.
    Sponsors
    We thank Geoffrey McFadden for providing anti-ACP antibody, J. Lapointe and A. Weiner for plasmids expressingCCA-adding enzyme, and Y. M. Hou for the pGFIB vector. We thankMR4 for providing P. falciparum 3D7 parasites contributed by DanCarucci and Alister Craig. The unpublished P. berghei genomesequence data were produced by the Pathogen Sequencing Group atthe Wellcome Trust Sanger Institute and can be obtained on line. Theunpublished C. velia and V. brassicaformis ortholog sequences weregraciously provided by Arnab Pain and Hifzur Ansari of King AbdullahUniversity of Science and Technology. The Chromera and Vitrellasequencing project was funded by a King Abdullah University of Scienceand Technology OCRF (GCR) award (FIC/2010/09) to ArnabPain. We also thank Jonathan Eisen and Dongying Wu for their consultingon the phylogenetic analyses.
    Publisher
    American Society for Biochemistry & Molecular Biology (ASBMB)
    Journal
    Journal of Biological Chemistry
    DOI
    10.1074/jbc.m115.655100
    PubMed ID
    26318454
    ae974a485f413a2113503eed53cd6c53
    10.1074/jbc.m115.655100
    Scopus Count
    Collections
    Publications Acknowledging KAUST Support

    entitlement

    Related articles

    • A nondiscriminating glutamyl-tRNA synthetase in the plasmodium apicoplast: the first enzyme in an indirect aminoacylation pathway.
    • Authors: Mailu BM, Ramasamay G, Mudeppa DG, Li L, Lindner SE, Peterson MJ, DeRocher AE, Kappe SH, Rathod PK, Gardner MJ
    • Issue date: 2013 Nov 8
    • On the evolution of the tRNA-dependent amidotransferases, GatCAB and GatDE.
    • Authors: Sheppard K, Söll D
    • Issue date: 2008 Mar 28
    • Biogenesis of glutaminyl-mt tRNAGln in human mitochondria.
    • Authors: Nagao A, Suzuki T, Katoh T, Sakaguchi Y, Suzuki T
    • Issue date: 2009 Sep 22
    • A dual-specific Glu-tRNA(Gln) and Asp-tRNA(Asn) amidotransferase is involved in decoding glutamine and asparagine codons in Acidithiobacillus ferrooxidans.
    • Authors: Salazar JC, Zúñiga R, Raczniak G, Becker H, Söll D, Orellana O
    • Issue date: 2001 Jul 6
    • Dual-targeted tRNA-dependent amidotransferase ensures both mitochondrial and chloroplastic Gln-tRNAGln synthesis in plants.
    • Authors: Pujol C, Bailly M, Kern D, Maréchal-Drouard L, Becker H, Duchêne AM
    • Issue date: 2008 Apr 29
    DSpace software copyright © 2002-2021  DuraSpace
    Quick Guide | Contact Us | Send Feedback
    Open Repository is a service hosted by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items. For anonymous users the allowed maximum amount is 50 search results.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.