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Reference: Louvion JF, et al. (1996) Two eukaryote-specific regions of Hsp82 are dispensable for its viability and signal transduction functions in yeast. Proc Natl Acad Sci U S A 93(24):13937-42

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Abstract

The 90-kDa heat shock protein (Hsp90) is a molecular chaperone that is very abundant even at normal temperature. It is highly conserved and essential for viability in yeast. To delineate functional domains of Hsp90, we have performed a deletion analysis of one of the two Hsp90 isoforms from budding yeast, Hsp82. The Hsp82 derivatives were tested for complementation of a Hsp90-deficient yeast strain and for their ability to function in two signal transduction pathways that depend on Hsp90. Surprisingly, we found that two salient features of Hsp90 sequences from eukaryotes, the N-terminal charged domain and the extremely conserved C-terminal pentapeptide MEEVD, are dispensable for viability as well as for proper regulation of vertebrate steroid receptors and for pheromone signaling. Moreover, we describe, to our knowledge, the first dominant negative mutant of Hsp90; A Hsp82 derivative that lacks amino acids 538-552 fails to complement but has a dominant negative effect on viability of wild-type strains at moderately elevated temperatures. This mutant may become a valuable tool to study Hsp90 functions both in yeast and in mammalian cells.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Louvion JF, Warth R, Picard D
Primary Lit For
HSP82
Additional Lit For
hsp82-(Δ538-552)

Phenotype Annotations 1 entry for 1 gene

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GenePhenotypeExperiment TypeMutant InformationStrain BackgroundChemicalDetails
HSP82heat sensitivity: increased
classical genetics dominant negative
Allele: hsp82-(Δ538-552)

toxic effect only apparent upon exposure to elevated temperatures, is neutralized by osmotic stabilizers; has no effect on short-term survival of cells upon heat shock

OtherTemperature: restrictive temperature, 38 °C
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