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Biochem J. 1995 Aug 15;310 ( Pt 1):225-32.

High constitutive levels of heat-shock proteins in human-pathogenic parasites of the genus Leishmania.

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1
Leishmaniasis Research Group, Bernhard Nocht Institute for Tropical Medicine, Hamburg, Federal Republic of Germany.

Abstract

We have analysed the transcription of three heat-shock genes, HSP70, HSP83 and ClpB, in the protozoan parasite Leishmania. All three heat-shock genes are transcribed constitutively and not heat-inducibly. However, we find that two major heat-shock proteins, HSP70 and HSP83, are synthesized at elevated rates during heat stress. We conclude that the cellular stress response in Leishmaniae is regulated exclusively on a post-transcriptional level much in contrast with all other eukaryotes examined so far. The induced synthesis of HSP70 and HSP83, however, does not increase the steady-state level of either protein significantly. This is compensated by high constitutive levels of both proteins: HSP70 and HSP83 make up 2.1% and 2.8%, respectively, of the total protein in unstressed Leishmania promastigotes. Also, HSP70 is a strictly cytoplasmic protein in Leishmania and does not relocate into the nucleus during heat stress, as it does in other eukaryotes examined in the past.

PMID:
7646449
PMCID:
PMC1135877
DOI:
10.1042/bj3100225
[Indexed for MEDLINE]
Free PMC Article

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