Characterization of NUDIX Hydrolase from Leishmania major
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Hydrolysis of a wide range of organic pyrophosphates is carried out by a family of NUDIX hydrolases present ubiquitously in all kingdoms of life. NUDIX hydrolases have a highly conserved 23 amino acid long NUDIX box domain. When the genome sequence of Leishmania major , was analyzed for NUDIX motif, it revealed nine proteins had NUDIX box domain. One of the gene products, encoded by LmjF .31.2950 ( Lm NH), had additional motifs like NADH pyrophosphatase zinc ribbon domain and a canonical peroxisomal targeting sequence type-1 (PTS-1). Expression of GFP fusion protein with C-terminally cloned Lm NH, in L. major , showed the fusion protein is targeted to microbody organelles as seen by the punctuate fluorescence. Proteomic analysis of purified glycosomes from L. major showed the presence of a single peptide with complete homology to Lm NH. Complementation assay in mutT defective Escherichia coli confirmed the ‘anti-mutator’ function of Lm NH. This preliminary report indicates that Lm NH may play an important role in the nucleotide metabolism in L. major glycosomes.
