NDLI: Plasmodium Apicoplast Gln-tRNAGln Biosynthesis Utilizes a Unique GatAB Amidotransferase Essential for Erythrocytic Stage Parasites.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Gardner, Malcolm J. Nelson, Todd M. Arthur, Jen Mailu, Boniface M. Li, Ling Becker, Katja Fritz-wolf, Karin Ramasamy, Gowthaman
Description	Author Affiliation: Mailu BM ( From the Center for Infectious Disease Research, Seattle, Washington 98109.); Li L ( From the Center for Infectious Disease Research, Seattle, Washington 98109.); Arthur J ( From the Center for Infectious Disease Research, Seattle, Washington 98109.); Nelson TM ( From the Center for Infectious Disease Research, Seattle, Washington 98109.); Ramasamy G ( From the Center for Infectious Disease Research, Seattle, Washington 98109.); Fritz-Wolf K ( the Department of Biochemistry and Molecular Biology, Interdisciplinary Research Center, Justus Liebig University, Giessen 35392 Germany, and the Max-Planck Institute for Medical Research, Jahnstrasse 29, D-69120 Heidelberg, Germany.); Becker K ( the Department of Biochemistry and Molecular Biology, Interdisciplinary Research Center, Justus Liebig University, Giessen 35392 Germany, and.); Gardner MJ ( From the Center for Infectious Disease Research, Seattle, Washington 98109, the Department of Global Health, University of Washington, Seattle, Washington 98195, mjgardner1@mac.com.)
Abstract	The malaria parasite Plasmodium falciparum apicoplast indirect aminoacylation pathway utilizes a non-discriminating glutamyl-tRNA synthetase to synthesize Glu-tRNA(Gln) and a glutaminyl-tRNA amidotransferase to convert Glu-tRNA(Gln) to Gln-tRNA(Gln). Here, we show that Plasmodium falciparum and other apicomplexans possess a unique heterodimeric glutamyl-tRNA 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-tRNA(Gln) to Gln-tRNA(Gln) 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.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	49
Volume Number	290
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2015-12-04
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Apicoplasts Metabolism GATA Transcription Factors Nitrogenous Group Transferases Plasmodium Falciparum Protozoan Proteins RNA, Transfer, Amino Acyl Biosynthesis Antimalarials Chemistry Cell Nucleus Computational Biology Erythrocytes Parasitology Gene Deletion Green Fluorescent Proteins Malaria Models, Molecular Phylogeny Protein Structure, Tertiary RNA, Transfer, Gln Genetics Recombinant Proteins Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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