ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

Characterization of coproporphyrinogen III oxidase in Plasmodium falciparum cytosol

Nagaraj, Viswanathan Arun and Prasad, Dasari and Arumugam, Rajavel and Rangarajan, Pundi N. and Padmanaban, Govindarajan (2010) Characterization of coproporphyrinogen III oxidase in Plasmodium falciparum cytosol. In: Parasitology International, 59 (2). pp. 121-127.

[img] PDF
Character.pdf - Published Version
Restricted to Registered users only

Download (1140Kb) | Request a copy
Official URL: http://dx.doi.org/10.1016/j.parint.2009.12.001

Abstract

A unique hybrid pathway has been proposed for de novo heme biosynthesis in Plasmodium falciparum involving three different compartments of the parasite, namely mitochondrion, apicoplast and cytosol. While parasite mitochondrion and apicoplast have been shown to harbor key enzymes of the pathway, there has been no experimental evidence for the involvement of parasite cytosol in heme biosynthesis. In this study, a recombinant P. falciparum coproporphyrinogen III oxidase (rPfCPO) was produced in E. coli and confirmed to be active under aerobic conditions. rPfCPO behaved as a monomer of 61 kDa molecular mass in gel filtration analysis. Immunofluorescence studies using antibodies to rPfCPO suggested that the enzyme was present in the parasite cytosol. These results were confirmed by detection of enzyme activity only in the parasite soluble fraction. Western blot analysis with anti-rPfCPO antibodies also revealed a 58 kDa protein only in this fraction and not in the membrane fraction. The cytosolic presence of PfCPO provides evidence for a hybrid heme-biosynthetic pathway in the malarial parasite. (C) 2009 Elsevier Ireland Ltd. All rights reserved.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Elsevier Science .
Keywords: Coproporphyrinogen III oxidase; Plasmodium falciparum; Heme
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 11 Nov 2010 10:33
Last Modified: 11 Nov 2010 10:33
URI: http://eprints.iisc.ernet.in/id/eprint/33542

Actions (login required)

View Item View Item