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J. Biol. Chem., Vol. 276, Issue 9, 6516-6523, March 2, 2001
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From the Sulfur-containing amino acids play an important
role in a variety of cellular functions such as protein synthesis,
methylation, and polyamine and glutathione synthesis. We cloned and
characterized cDNA encoding cystathionine The nucleotide sequence reported in this paper has been submitted
to the DDBJ/GenBankTM/EBI Data Bank with
accession numbers AF296842-AF296848.
Characterization of Transsulfuration and Cysteine Biosynthetic
Pathways in the Protozoan Hemoflagellate, Trypanosoma
cruzi
ISOLATION AND MOLECULAR CHARACTERIZATION OF CYSTATHIONINE
-SYNTHASE AND SERINE ACETYLTRANSFERASE FROM
TRYPANOSOMA*
§,,,, and Department of Parasitology, National
Institute of Infectious Diseases, 1-23-1 Toyama, Shinjuku-ku, Tokyo
162-8640, Japan and the ¶ Division of Population Sciences, Fox
Chase Cancer Center, Philadelphia, Pennsylvania 19111
-synthase (CBS), which
is a key enzyme of transsulfuration pathway, from a hemoflagellate
protozoan parasite Trypanosoma cruzi. T. cruzi CBS, unlike
mammalian CBS, lacks the regulatory carboxyl terminus, does not contain
heme, and is not activated by S-adenosylmethionine.
T. cruzi CBS mRNA is expressed as at least six
independent isotypes with sequence microheterogeneity from tandemly
linked multicopy genes. The enzyme forms a homotetramer and, in
addition to CBS activity, the enzyme has serine sulfhydrylase and
cysteine synthase (CS) activities in vitro. Expression of the T. cruzi CBS in Saccharomyces cerevisiae
and Escherichia coli demonstrates that the CBS and CS
activities are functional in vivo. Enzymatic studies on
T. cruzi extracts indicate that there is an additional CS
enzyme and stage-specific control of CBS and CS expression. We also
cloned and characterized cDNA encoding serine acetyltransferase
(SAT), a key enzyme in the sulfate assimilatory cysteine biosynthetic
pathway. Dissimilar to bacterial and plant SAT, a recombinant T. cruzi SAT showed allosteric inhibition by L-cysteine,
L-cystine, and, to a lesser extent, glutathione. Together, these studies demonstrate the T. cruzi is a unique protist
in possessing both transsulfuration and sulfur assimilatory pathways.
*
This work was supported by Grant-in-aid 11770132 from the
Ministry of Education, Culture, Sports, Science and Technology of Japan, by grants for research on emerging and re-emerging infectious diseases from the Ministry of Health, Labour and Welfare of Japan, and
by Grant K-1037 from Japan Health Sciences Foundation for research on
health sciences focusing on drug innovation.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.
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