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J Biol Chem, Vol. 273, Issue 11, 6488-6494, March 13, 1998
From the Leishmaniasis Unit, Bernhard Nocht Institute for
Tropical Medicine, 20359 Hamburg, Germany
We report the cloning and molecular
analysis of the Leishmania donovani clpB gene. The
protein-coding region is highly conserved compared with its L. major homologue, while 5'- and 3'-flanking DNA sequences display
considerable divergence. The encoded mRNA has an unusually long
5'-leader sequence typical for RNAs, which are translated
preferentially under heat stress. The gene product, a 100-kDa heat
shock protein, Hsp100, becomes abundant only during sustained heat
stress, but not under common chemical stresses. Hsp100 associates into
trimeric complexes and is found mostly in a cytoplasmic, possibly
membrane-associated, localization as determined by immune electron
microscopy. Hsp100 shows immediate early expression kinetics during
axenic amastigote development. In its absence, expression of at least
one amastigote stage-specific protein family is impaired.
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