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Journal of Cell Science, Vol 104, Issue 4 1091-1100, Copyright © 1993 by Company of Biologists

JOURNAL ARTICLES

Expression of a mitochondrial stress protein in the protozoan parasite Leishmania major

S Searle, MV McCrossan and DF Smith
Department of Biochemistry, Imperial College of Science, Technology and Medicine, London, UK.

The DNA sequence has been determined of a gene from Leishmania major that shares sequence identity with members of the eukaryotic heat shock protein (hsp) 70 gene family. The deduced open reading frame for translation shares a number of features common to hsp70 stress proteins, including conserved amino acids implicated in ATP binding and a putative 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 constitutively expressed and localises to the mitochondrion in all stages of the parasite life cycle. These features suggest a role for this protein as a molecular chaperone in Leishmania.
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© The Company of Biologists Ltd 1993