EXPRESSION OF A MITOCHONDRIAL STRESS PROTEIN IN THE PROTOZOAN PARASITE LEISHMANIA-MAJOR

The DNA sequence has been determined of a gene from Leishmania major t hat shares sequence identity with members of the eukaryotic heat shock protein (hsp) 70 gene family. The deduced open reading frame for tran slation shares a number of features common to hsp70 stress proteins, i ncluding conserved amino acids implicated in ATP binding and a putativ e calmodulin-binding site. In addition, the protein has an N-terminal sequence characteristic of a mitochondrial targeting signal. Specific antibodies to this Protein, generated by the use of recombinant fusion peptides, recognise a 65 kDa molecule of pI 6.7. This molecule is con stitutively expressed and localises to the mitochondrion in all stages of the parasite life cycle. These features suggest a role for this pr otein as a molecular chaperone in Leishmania.