Leishmania major: characterisation and expression of a cytoplasmic stress-related protein.
The DNA sequence of a single-copy gene from Leishmania major has been determined and shown to share sequence identity with eukaryotic heat shock protein-70-related genes. Conserved features of the deduced open reading frame include amino acids implicated in ATP binding and a putative calmodulin-binding domain. Antibodies generated to the recombinant fusion protein recognise a 70-kDa molecule of pI 6.0. This molecule is constitutively expressed and localises to the cytoplasm in all stages of the parasite life cycle.
Searle
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Department of Biochemistry, Imperial College of Science, Technology and Medicine, London, U.K.
Smith
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D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002467:Cell Nucleus / Q000737:chemistry; D003593:Cytoplasm / Q000737:chemistry; D017125:Genes, Protozoan; D006360:Heat-Shock Proteins / Q000032:analysis / Q000737:chemistry / Q000235:genetics*; D006358:Hot Temperature; D007895:Leishmania tropica / Q000737:chemistry / Q000235:genetics*; D008856:Microscopy, Fluorescence; D016253:Microscopy, Immunoelectron; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D015800:Protozoan Proteins / Q000032:analysis / Q000737:chemistry / Q000235:genetics*; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis; D016415:Sequence Alignment; D017421:Sequence Analysis
D006360:Heat-Shock Proteins; D015800:Protozoan Proteins; D011993:Recombinant Fusion Proteins; C082489:hsp70.4 protein, Leishmania major