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J. Biol. Chem., Vol. 276, Issue 8, 5483-5490, February 23, 2001
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From Fachbereich Biologie/Parasitologie,
Philipps-Universität Marburg, Karl-von-Frisch-Strasse, 35032 Marburg, Germany
In searching for nuclear-encoded,
apicoplast-localized proteins we have cloned
ferredoxin-NADP+ reductase from Toxoplasma
gondii and a [2Fe-2S] ferredoxin from Plasmodium
falciparum. This chloroplast-localized redox system has been
extensively studied in photosynthetic organisms and is responsible for
the electron transfer from photosystem I to NADP+. Besides
this light-dependent reaction in nonphotosynthetic plastids (e.g. from roots), electrons can also flow in the reverse
direction, from NADPH to ferredoxin, which then serves as an important
reductant for various plastid-localized enzymes. These plastids possess related, but distinct, ferredoxin-NADP+ reductase and
ferredoxin isoforms for this purpose. We provide phylogenetic evidence
that the T. gondii reductase is similar to such
nonphotosynthetic isoforms. Both the P. falciparum
[2Fe-2S] ferredoxin and the T. gondii
ferredoxin-NADP+ reductase possess an N-terminal bipartite
transit peptide domain typical for apicoplast-localized proteins. The
recombinant proteins were obtained in active form, and antibodies
raised against the reductase recognized two bands on Western blots of
T. gondii tachyzoite lysates, indicative of the unprocessed
and native form, respectively. We propose that the role of this redox
system is to provide reduced ferredoxin, which might then be used for
fatty acid desaturation or other biosynthetic processes yet to be
defined. Thus, the interaction of these two proteins offers an
attractive target for drug intervention.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AJ242627 (for T. gondii FNR).
Apicomplexan Parasites Possess Distinct Nuclear-encoded, but
Apicoplast-localized, Plant-type Ferredoxin-NADP+
Reductase and Ferredoxin*
*
This work was supported in part by a grant from the Deutsche
Forschungsgemeinschaft (to F. S.) (Se622-3/2). Sequencing of P. falciparum chromosomes 9 and 13 was accomplished as part
of the Malaria Genome Project with support by The Wellcome
Trust.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 49-6421-2826596;
Fax: 49-6421-2821531; E-mail
seeber@mailer.uni-marburg.de.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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