TAILIEUCHUNG - Báo cáo khoa học: A FYVE-containing unusual cyclic nucleotide phosphodiesterase from Trypanosoma cruzi

Cyclic-nucleotide-specific phosphodiesterases (PDEs) are key players in the intracellular signaling pathways of the important human pathogen Trypano-soma cruzi. We report herein the identification of an unusual PDE from this protozoal organism. This enzyme, TcrPDEC, is a member of the class I PDEs, as determined from the presence of a characteristic signature sequence and from the conservation of a number of functionally important amino acid residues within its catalytic domain. | iFEBS Journal A FYVE-containing unusual cyclic nucleotide phosphodiesterase from Trypanosoma cruzi Stefan Kunz Michael Oberholzer and Thomas Seebeck Institute of CellBiology University of Bern Bern Switzerland Keywords Chagas disease cyclic nucleotides FYVE domain kinetoplastids phosphodiesterase Correspondence T. Seebeck Institute of Cell Biology Baltzerstrasse 4 CH-3012 BERN Switzerland Fax 41 31 6314684 Tel 41 31 6314649 E-mail Website http Nucleotide sequence data have been submitted to the DDBJ EMBL GenBank databases under the accession numbers AJ889575 and AJ889576 for TcrPDEC alleles 1 and 2 respectively. Received 26 August 2005 revised 20 October 2005 accepted 27 October 2005 doi Cyclic-nucleotide-specific phosphodiesterases PDEs are key players in the intracellular signaling pathways of the important human pathogen Trypanosoma cruzi. We report herein the identification of an unusual PDE from this protozoal organism. This enzyme TcrPDEC is a member of the class I PDEs as determined from the presence of a characteristic signature sequence and from the conservation of a number of functionally important amino acid residues within its catalytic domain. Class I PDEs include a large number of PDEs from eukaryotes among them all 11 human PDE families. Unusually for an enzyme of this class TcrPDEC contains a FYVE-type domain in its N-terminal region followed by two closely spaced coiled-coil domains. Its catalytic domain is located in the middle of the polypeptide chain whereas all other class I enzymes contain their catalytic domains in their C-terminal parts. TcrPDEC can complement a PDE-deficient yeast strain. Unexpectedly for a kinetoplastid PDE TcrPDEC is a dual-specificity PDE that accepts both cAMP and cGMP as its substrates. The cell biology of Trypanosoma cruzi the causative agent of South American Chagas disease has been extensively studied. Surprisingly still very little is .

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