Pyruvate kinase type-II isozyme in Plasmodium falciparum localizes to the apicoplast

Takuya Maeda; Tomoya Saito; Omar S. Harb; David S. Roos; Satoru Takeo; Hiroko Suzuki; Takafumi Tsuboi; Tsutomu Takeuchi; Takashi Asai

doi:10.1016/j.parint.2008.10.005

Pyruvate kinase type-II isozyme in Plasmodium falciparum localizes to the apicoplast

Takuya Maeda, Tomoya Saito, Omar S. Harb, David S. Roos, Satoru Takeo, Hiroko Suzuki, Takafumi Tsuboi, Tsutomu Takeuchi, Takashi Asai

Research output: Contribution to journal › Article › peer-review

26 Citations (Scopus)

Abstract

Bioinformatics research on Plasmodium falciparum revealed two isoforms of pyruvate kinase: type-I and type-II enzymes. The type-I enzyme shows typical glycolytic properties, while type-II enzyme is involved in fatty acid type-II biosynthesis and has been predicted to localize to the apicoplast with the targeting signal in its N-terminus. The type-I and type-II isoforms have the same evolutionary origin as Toxoplasma gondii isozymes, TgPyKI and TgPyKII, respectively; however, TgPyKII localizes to both the mitochondrion and the apicoplast. Accordingly, we made a recombinant full length of P. falciparum pyruvate kinase type-II protein using a wheat germ cell-free expression system and obtained a specific antibody against the type-II protein. Fluorescent microscopic analysis revealed that P. falciparum type-II enzyme was localized only to the apicoplast, not to the mitochondrion. The data suggest differences in localization and metabolic pathways between P. falciparum and T. gondii pyruvate kinase isoforms.

Original language	English
Pages (from-to)	101-105
Number of pages	5
Journal	Parasitology International
Volume	58
Issue number	1
DOIs	https://doi.org/10.1016/j.parint.2008.10.005
Publication status	Published - 2009 Mar
Externally published	Yes

Keywords

Apicoplast
Cell-free expression
Mitochondria
Plasmodium falciparum
Pyruvate kinase II

ASJC Scopus subject areas

Parasitology
Infectious Diseases

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.parint.2008.10.005

Cite this

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title = "Pyruvate kinase type-II isozyme in Plasmodium falciparum localizes to the apicoplast",

abstract = "Bioinformatics research on Plasmodium falciparum revealed two isoforms of pyruvate kinase: type-I and type-II enzymes. The type-I enzyme shows typical glycolytic properties, while type-II enzyme is involved in fatty acid type-II biosynthesis and has been predicted to localize to the apicoplast with the targeting signal in its N-terminus. The type-I and type-II isoforms have the same evolutionary origin as Toxoplasma gondii isozymes, TgPyKI and TgPyKII, respectively; however, TgPyKII localizes to both the mitochondrion and the apicoplast. Accordingly, we made a recombinant full length of P. falciparum pyruvate kinase type-II protein using a wheat germ cell-free expression system and obtained a specific antibody against the type-II protein. Fluorescent microscopic analysis revealed that P. falciparum type-II enzyme was localized only to the apicoplast, not to the mitochondrion. The data suggest differences in localization and metabolic pathways between P. falciparum and T. gondii pyruvate kinase isoforms.",

keywords = "Apicoplast, Cell-free expression, Mitochondria, Plasmodium falciparum, Pyruvate kinase II",

author = "Takuya Maeda and Tomoya Saito and Harb, {Omar S.} and Roos, {David S.} and Satoru Takeo and Hiroko Suzuki and Takafumi Tsuboi and Tsutomu Takeuchi and Takashi Asai",

note = "Funding Information: We thank Dr. Shinichiro Kawazu (Obihiro University of Agriculture and Veterinary Medical) for providing genomic DNA of P. falciparum , and Dr. Geoffrey I. McFadde (University of Melbourne) for providing both anti-acyl carrier protein rabbit antibody and P. falciparum expressing citrate synthase fused to GFP. This work was supported in part by Keio Gijuku Academic Development Funds, Japan.",

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doi = "10.1016/j.parint.2008.10.005",

language = "English",

volume = "58",

pages = "101--105",

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T1 - Pyruvate kinase type-II isozyme in Plasmodium falciparum localizes to the apicoplast

AU - Maeda, Takuya

AU - Saito, Tomoya

AU - Harb, Omar S.

AU - Roos, David S.

AU - Takeo, Satoru

AU - Suzuki, Hiroko

AU - Tsuboi, Takafumi

AU - Takeuchi, Tsutomu

AU - Asai, Takashi

N1 - Funding Information: We thank Dr. Shinichiro Kawazu (Obihiro University of Agriculture and Veterinary Medical) for providing genomic DNA of P. falciparum , and Dr. Geoffrey I. McFadde (University of Melbourne) for providing both anti-acyl carrier protein rabbit antibody and P. falciparum expressing citrate synthase fused to GFP. This work was supported in part by Keio Gijuku Academic Development Funds, Japan.

PY - 2009/3

Y1 - 2009/3

N2 - Bioinformatics research on Plasmodium falciparum revealed two isoforms of pyruvate kinase: type-I and type-II enzymes. The type-I enzyme shows typical glycolytic properties, while type-II enzyme is involved in fatty acid type-II biosynthesis and has been predicted to localize to the apicoplast with the targeting signal in its N-terminus. The type-I and type-II isoforms have the same evolutionary origin as Toxoplasma gondii isozymes, TgPyKI and TgPyKII, respectively; however, TgPyKII localizes to both the mitochondrion and the apicoplast. Accordingly, we made a recombinant full length of P. falciparum pyruvate kinase type-II protein using a wheat germ cell-free expression system and obtained a specific antibody against the type-II protein. Fluorescent microscopic analysis revealed that P. falciparum type-II enzyme was localized only to the apicoplast, not to the mitochondrion. The data suggest differences in localization and metabolic pathways between P. falciparum and T. gondii pyruvate kinase isoforms.

AB - Bioinformatics research on Plasmodium falciparum revealed two isoforms of pyruvate kinase: type-I and type-II enzymes. The type-I enzyme shows typical glycolytic properties, while type-II enzyme is involved in fatty acid type-II biosynthesis and has been predicted to localize to the apicoplast with the targeting signal in its N-terminus. The type-I and type-II isoforms have the same evolutionary origin as Toxoplasma gondii isozymes, TgPyKI and TgPyKII, respectively; however, TgPyKII localizes to both the mitochondrion and the apicoplast. Accordingly, we made a recombinant full length of P. falciparum pyruvate kinase type-II protein using a wheat germ cell-free expression system and obtained a specific antibody against the type-II protein. Fluorescent microscopic analysis revealed that P. falciparum type-II enzyme was localized only to the apicoplast, not to the mitochondrion. The data suggest differences in localization and metabolic pathways between P. falciparum and T. gondii pyruvate kinase isoforms.

KW - Apicoplast

KW - Cell-free expression

KW - Mitochondria

KW - Plasmodium falciparum

KW - Pyruvate kinase II

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Pyruvate kinase type-II isozyme in Plasmodium falciparum localizes to the apicoplast

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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