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J. Biol. Chem., Vol. 277, Issue 43, 41171-41182, October 25, 2002

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Identification and Characterization of Moca-cyp
A DROSOPHILA MELANOGASTER NUCLEAR CYCLOPHILIN^*

Laurent Cavarec^§¶, Thilo Kamphausen, Bérangère Dubourg^¶, Isabelle Callebaut^**, Françoise Lemeunier, Didier Métivier, Jean Feunteun, Gunter Fischer, and Nazanine Modjtahedi^§§

From the  Laboratoire de Génétique Oncologique, UMR1599, Institut Gustave Roussy-PR1, 39 rue Camille Desmoulins, Villejuif 94805 cedex, France, the  Max-Planck Forschungsstelle "Enzymologie der Proteinfaltung," Weinbergweg 22, Halle/Saale D-06120, Germany, the ^** Systèmes moléculaires et Biologie structurale, Laboratoire de Minéralogie et Cristallographie de Paris, CNRS UMR7590, Universités Paris 6 & 7, case 115, 4 place Jussieu, Paris 75252 cedex 05, France, and the  Laboratoire Populations, Génétique et Evolution, CNRS, Gif-sur-Yvette 91198 cedex, France

Cyclophilins are enzymes catalyzing the cis-trans isomerization of peptidyl-prolyl bonds and belong to the enzyme class of peptidyl-prolyl cis-trans isomerases (PPIases), which includes two more families (FK506 binding proteins and parvulins). We report the characterization of a novel cyclophilin (Moca-cyp) isolated from Drosophila melanogaster. The single-copy Moca-cyp gene, which is localized on chromosome 3R, was cloned and sequenced. The sequence alignment of the gene against Moca-cyp cDNA allowed us to define its intron/exon structure and to identify a variant cDNA corresponding to an alternatively spliced mRNA. By embryo in situ RNA hybridization and immunostaining, we show that the expression of Moca-cyp is regulated during embryogenesis of Drosophila. The 120-kDa nuclear Moca-cyp protein belongs to a subfamily of large cyclophilins sharing structural and enzymatic features: their highly conserved N-terminal PPIase domain is extended by a positively charged and divergent C-terminal tail. Compared with cyclophilin 18, the enzymatic activity carried by the PPIase domain of Moca-cyp is low, exhibits characteristic substrate specificity, and shows a reduced sensitivity to the drug cyclosporin A (CsA). The reduced affinity for CsA is one of the typical features linking members of this subfamily and is probably the consequence of two amino acid substitutions within their active site. Another structural feature shared by members of this subfamily is a conserved polypeptidic segment ("moca" domain) that we report for the first time. The moca domain is located within the C-terminal tail and is the exclusive hallmark of a group of large cyclophilins found in multicellular organisms of the animal kingdom.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AY134669.

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