Journal article

Publication year: 2015

Pages: 29629-29641

Journal: Journal of Biological Chemistry

Volume number: 290

Issue number: 49

ISSN: 0021-9258

eISSN: 1083-351X

Open access status: Green

DOI Link: https://doi.org/10.1074/jbc.M115.655100

Publisher: Elsevier

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.

Harvard Citation style: Mailu, B., Li, L., Arthur, J., Nelson, T., Ramasamy, G., Fritz-Wolf, K., et al. (2015) Plasmodium Apicoplast Gln-tRNA(Gln) Biosynthesis Utilizes a Unique GatAB Amidotransferase Essential for Erythrocytic Stage Parasites, Journal of Biological Chemistry, 290(49), pp. 29629-29641. https://doi.org/10.1074/jbc.M115.655100

APA Citation style: Mailu, B., Li, L., Arthur, J., Nelson, T., Ramasamy, G., Fritz-Wolf, K., Becker, K., & Gardner, M. (2015). Plasmodium Apicoplast Gln-tRNA(Gln) Biosynthesis Utilizes a Unique GatAB Amidotransferase Essential for Erythrocytic Stage Parasites. Journal of Biological Chemistry. 290(49), 29629-29641. https://doi.org/10.1074/jbc.M115.655100