Expression of a mitochondrial stress protein in the protozoan parasite Leishmania major.
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.
Searle
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S
Department of Biochemistry, Imperial College of Science, Technology and Medicine, London, UK.
McCrossan
M V
MV
Smith
D F
DF
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015870:Gene Expression; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000096:biosynthesis*; D007895:Leishmania tropica / Q000378:metabolism* / Q000648:ultrastructure; D008928:Mitochondria / Q000378:metabolism*; D008969:Molecular Sequence Data; D015800:Protozoan Proteins / Q000096:biosynthesis*; D016415:Sequence Alignment
D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D015800:Protozoan Proteins; C081884:heat-shock protein 70.1