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J Biol Chem, Vol. 275, Issue 2, 1495-1501, January 14, 2000
From the Instituto de Investigaciones en Ingeniería
Genética y Biología Molecular, Consejo Nacional de
Investigaciones Científicas y Técnicas, and Facultad de
Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos
Aires, Argentina
This work contains the first description of a
guanidino kinase in a flagellar unicellular parasite. The enzyme
phosphorylates L-arginine and was characterized in
preparations from Trypanosoma cruzi, the ethiological agent
of Chagas' disease. The activity requires ATP and a divalent cation.
Under standard assay conditions (1 mM
L-arginine), the presence of 5-fold higher concentrations of canavanine or histidine produced a greater than 50% enzyme inhibition. The base sequence of this enzyme revealed an open reading
frame of 357 amino acids and a molecular weight of 40,201. The amino
acid sequence shows all of the characteristic consensus blocks of the
ATP:guanidino phosphotransferase family and a putative "actinin-type" actin-binding domain. The highest amino acid
identities of the T. cruzi sequence, about 70%, were with
arginine kinases from Arthropoda. Southern and chromosome blots
revealed that the kinase is encoded by a single-copy gene. Moreover,
Northern blot analysis showed an mRNA subpopulation of about 2.0 kilobases, and Western blotting of T. cruzi-soluble
polypeptides revealed a 40-kDa band. The finding in the parasite of a
phosphagen and its biosynthetic pathway, which are totally different
from those in mammalian host tissues, points out this arginine kinase
as a possible chemotherapy target for Chagas' disease.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF070451, AI035059, AF023619, P48610,
P51545, Q27535, AE001338, P00732, P12277, P51546, and O15991.
Trypanosoma cruzi Arginine Kinase Characterization
and Cloning
A NOVEL ENERGETIC PATHWAY IN PROTOZOAN PARASITES*
*
This study was supported in part by the Consejo Nacional de
Investigaciones Científicas y Técnicas (Argentina), the
University of Buenos Aires (Argentina), the Agencia Nacional de
Promoción Científica y Tecnológica (Argentina), the
International Center for Genetic Engineering and Biotechnology
(Trieste, Italy), and the Argentine-Brazilian Center for Biotechnology.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: INGEBI, Vuelta de
Obligado 2490, 1428 Buenos Aires, Argentina. Tel.: 54-11-4783-2871; Fax: 54-11-4786-8578; E-mail: mflawia@proteus.dna.uba.ar.
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