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Subcellular localization of Trypanosoma cruzi arginine kinase

Published online by Cambridge University Press:  27 July 2009

MARIANA R. MIRANDA
Affiliation:
Laboratorio de Biología Molecular de Trypanosoma cruzi (LBMTC), Instituto de Investigaciones Médicas (IDIM), CONICET and Universidad de Buenos Aires, Combatientes de Malvinas 3150, Buenos Aires, Argentina
LEÓN A. BOUVIER
Affiliation:
Laboratorio de Biología Molecular de Trypanosoma cruzi (LBMTC), Instituto de Investigaciones Médicas (IDIM), CONICET and Universidad de Buenos Aires, Combatientes de Malvinas 3150, Buenos Aires, Argentina
GASPAR E. CANEPA
Affiliation:
Laboratorio de Biología Molecular de Trypanosoma cruzi (LBMTC), Instituto de Investigaciones Médicas (IDIM), CONICET and Universidad de Buenos Aires, Combatientes de Malvinas 3150, Buenos Aires, Argentina
CLAUDIO A. PEREIRA*
Affiliation:
Laboratorio de Biología Molecular de Trypanosoma cruzi (LBMTC), Instituto de Investigaciones Médicas (IDIM), CONICET and Universidad de Buenos Aires, Combatientes de Malvinas 3150, Buenos Aires, Argentina
*
*Corresponding author: IDIM, Combatientes de Malvinas 3150, (1427) Bs. As., Argentina. Tel: +5411 4514 8701. Fax: +5411 4523 8904. E-mail: cpereira@mail.retina.ar

Summary

Phosphoarginine is a cell energy buffer molecule synthesized by the enzyme arginine kinase. In Trypanosoma cruzi, the aetiological agent of Chagas' disease, 2 different isoforms were identified by data mining, but only 1 was expressed during the parasite life cycle. The digitonin extraction pattern of arginine kinase differed from those obtained for reservosomes, glycosomes and mitochondrial markers, and similar to the cytosolic marker. Immunofluorescence analysis revealed that although arginine kinase is localized mainly in unknown punctuated structures and also in the cytosol, it did not co-localize with any of the subcelular markers. This punctuated pattern has previously been observed in many cytosolic proteins of trypanosomatids. The knowledge of the subcellular localization of phosphagen kinases is a crucial issue to understand their physiological role in protozoan parasites.

Type
Research Article
Copyright
Copyright © Cambridge University Press 2009

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