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J Biol Chem, Vol. 275, Issue 2, 1112-1118, January 14, 2000
From the Section of Infectious Diseases, Department of Internal
Medicine, Yale University School of Medicine,
New Haven, Connecticut 06520-8022
We sought to identify and characterize
peroxisomes in the apicomplexan parasite Toxoplasma gondii.
To initiate this process, we first cloned and sequenced the gene for
T. gondii catalase (EC 1.11.1.6), a marker enzyme for
peroxisomes in eukaryotic cells. The gene predicts a protein of 57.2 kDa and 502 amino acids and has a strong homology to other eukaryotic
catalases. A polyclonal antiserum raised against a glutathione
S-transferase fusion protein recognized a single band with
a molecular mass of 63 kDa by immunoblot. By immunofluorescence
T. gondii catalase is present primarily in a punctate
staining pattern anterior to the parasite nucleus. This compartment is
distinguishable from other parasite organelles, namely micronemes,
rhoptries, dense granules, and the apicoplast. Cytochemical
visualization of catalase using diaminobenzidine precipitation gives a
vesicular staining pattern anterior to the nucleus at the light level
and round, vesicular structures with an estimated diameter of 100-300
nm by electron microscopy. T. gondii catalase has a
putative C-terminal peroxisomal targeting signal in the last 3 amino
acids (-AKM). Expression of T. gondii catalase in mammalian
cells results in peroxisomal localization, whereas a construct lacking
the targeting signal remains in the cytosol. Furthermore, addition of
-AKM to the C terminus of chloramphenicol acetyltransferase is
sufficient to target this protein to peroxisomes. These results provide
the first evidence for peroxisomes in Apicomplexan parasites.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF136344 and AF136344. The amino acid sequence of this protein can be accessed through
NCBI Protein Database under NCBI accession numbers 179950, 1078837, and
115709.
Targeting and Subcellular Localization of Toxoplasma
gondii Catalase
IDENTIFICATION OF PEROXISOMES IN AN APICOMPLEXAN PARASITE*
*
This work was supported by National Institutes of Health
Grant A130060 and a Burroughs Wellcome Scholar award in Molecular Parasitology (to K. A. J.).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: Infectious Diseases
Section, Dept. of Internal Medicine, 808 LCI, 333 Cedar St., New Haven,
CT 06520-8022. Tel.: 203-785-4140; Fax: 203-785-3864; E-mail:
keith.joiner@yale.edu.
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