PMID:9497383

Citation	Krobitsch, S, Brandau, S, Hoyer, C, Schmetz, C, Hübel, A and Clos, J (1998) Leishmania donovani heat shock protein 100. Characterization and function in amastigote stage differentiation. J. Biol. Chem. 273:6488-94
Abstract	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.
Links	PubMed
Keywords	Animals; Base Sequence; Cell Compartmentation; Cell Differentiation; Cloning, Molecular; Conserved Sequence; Gene Expression Regulation; Genes, Protozoan; Heat-Shock Proteins/genetics; Heat-Shock Proteins/isolation & purification; Heat-Shock Proteins/metabolism; Heat-Shock Response; Leishmania donovani/cytology; Leishmania donovani/genetics; Microscopy, Immunoelectron; Molecular Sequence Data; Protozoan Proteins/genetics; Protozoan Proteins/isolation & purification; Protozoan Proteins/metabolism; Sequence Analysis, DNA; Species Specificity
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
LEIDO:O00828		GO:0006950: response to stress	ECO:0000247:	PMID:9497383	P		Go to figure 1	complete CACAO 9196

References

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