Primary structure of the hydrogenosomal adenylate kinase of Trichomonas vaginalis and its phylogenetic relationships

Abstract

Hydrogenosomal adenylate kinase of the amitochondriate protist, Trichomonas vaginalis, has been purified and the sequence of its 39 amino-terminal residues established. Based on this sequence and a conserved internal region of the enzyme, a probe was obtained by DNA polymerase chain reaction and used to isolate a genomic DNA clone containing the gene of this enzyme. This gene exists probably as a single copy in T. vaginalis and is not interrupted by introns. The open reading frame obtained codes for a large type adenylate kinase with a mature molecular mass of 24.5 kDa. The T. vaginalis enzyme is homologous with adenylate kinases of other eukaryotes and eubacteria. Strongly conserved parts and residues of the molecule are conserved also in this enzyme. Phylogenetic trees obtained with various methods placed the T. vaginalis adenylate kinase close to the point where the different subfamilies of this enzyme branch from each other, indicating that the T. vaginalis enzyme has no close relationship to any of these subfamilies and that it separated early from other adenylate kinases. The conceptual translation predicts the existence of an amino-terminal nonapeptide absent from the protein purified from hydrogenosomes, similar to the processed amino-terminal extensions of other hydrogenosomal proteins. These extensions have been considered as putative targeting and import signals.