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J. Biol. Chem., Vol. 280, Issue 12, 11781-11789, March 25, 2005

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Intracellular Positioning of Isoforms Explains an Unusually Large Adenylate Kinase Gene Family in the Parasite Trypanosoma brucei^*

From the ^aSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford, OX1 3RE, United Kingdom, the ^cInterdisziplinäres Forschungszentrum, Justus-Liebig-Universität, Heinrich-Buff-Ring 26-32, 35392 Giessen, Germany, the ^dInstituto de Investigaciones Médicas Alfredo Lanari, Consejo Nacional de Investigaciones Científicas y Técnicas, Universidad de Buenos Aires, Buenos Aires 1427, Argentina, ^fHygiene-Institut der Ruprecht-Karls-Universität, Im Neuenheimer Feld 324, 69120 Heidelberg, Germany, and the ⁱSchool of Medicine, Health Policy, and Practice, University of East Anglia, Norwich, NR4 7TJ, United Kingdom

Adenylate kinases occur classically as cytoplasmic and mitochondrial enzymes, but the expression of seven adenylate kinases in the flagellated protozoan parasite Trypanosoma brucei (order, Kinetoplastida; family, Trypanosomatidae) easily exceeds the number of isoforms previously observed within a single cell and raises questions as to their location and function. We show that a requirement to target adenylate kinase into glycosomes, which are unique kinetoplastid-specific microbodies of the peroxisome class in which many reactions of carbohydrate metabolism are compartmentalized, and two different flagellar structures as well as cytoplasm and mitochondrion explains the expansion of this gene family in trypanosomes. The three isoforms that are selectively built into either the flagellar axoneme or the extra-axonemal paraflagellar rod, which is essential for motility, all contain long N-terminal extensions. Biochemical analysis of the only short form trypanosome adenylate kinase revealed that this enzyme catalyzes phosphotransfer of -phosphate from ATP to AMP, CMP, and UMP acceptors; its high activity and specificity toward CMP is likely to reflect an adaptation to very low intracellular cytidine nucleotide pools. Analysis of some of the phosphotransfer network using RNA interference suggests considerable complexity within the homeostasis of cellular energetics. The anchoring of specific adenylate kinases within two distinct flagellar structures provides a paradigm for metabolic organization and efficiency in other flagellates.

Received for publication, December 8, 2004 , and in revised form, January 14, 2005.

^* This work was supported in part by a Wellcome Trust program grant (to K. G., who is a Wellcome Trust Principal Research Fellow), by the Sonderforschungsbereich 544 der Deutschen Forschungsgemeinschaft (to D. S.), The Royal Society (to M. L. G., who is a Royal Society University Research Fellow), by a Forschungsstipendium für Experimentelle Parasitologie der Karl-Enigk-Stiftung (to E. N.), by the fundación Antorchas (to C. A. P.), and by a Biotechnology and Biological Sciences Research Council studentship (to T. J. P.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental data, including an additional table and figure.

^b Both authors contributed equally to the experimental work.

^e Supported in Oxford by the Royal Society.

^g Present address: Aventis Pharma, Mainzer Landstrasse 500, 65795 Hattersheim, Germany.

^h To whom correspondence may be addressed. Tel.: 44-1865-285455; Fax: 44-1865-285691; E-mail: keith.gull{at}pathology.oxford.ac.uk.

^j To whom correspondence may be addressed. Tel.: 44-1603-591291; Fax: 44-1603-593752; E-mail: dsteverding{at}hotmail.com.

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