Leishmania donovani Heat Shock Protein 100 CHARACTERIZATION AND FUNCTION IN AMASTIGOTE STAGE DIFFERENTIATION
作者： Sylvia Krobitsch , Sven Brandau , Cornelia Hoyer , Christel Schmetz , Andreas Hübel
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摘要: We report the cloning and molecular analysis of Leishmania donovani clpB gene. The protein-coding region is highly conserved compared with its L. major homologue, while 5'- 3'-flanking DNA sequences display considerable divergence. encoded mRNA has an unusually long 5'-leader sequence typical for RNAs, which are translated preferentially under heat stress. gene product, a 100-kDa shock protein, Hsp100, becomes abundant only during sustained stress, but not common chemical stresses. Hsp100 associates into trimeric complexes found mostly in cytoplasmic, possibly membrane-associated, localization as determined by immune electron microscopy. shows immediate early expression kinetics axenic amastigote development. In absence, at least one stage-specific protein family impaired.
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