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Identification and characterization of cytosolic Hansenula polymorpha proteins belonging to the Hsp70 protein family.

Authors
  • Titorenko, V I
  • Evers, M E
  • Diesel, A
  • Samyn, B
  • Van Beeumen, J
  • Roggenkamp, R
  • Kiel, J A
  • van der Klei, I J
  • Veenhuis, M
Type
Published Article
Journal
Yeast (Chichester, England)
Publication Date
Jul 01, 1996
Volume
12
Issue
9
Pages
849–857
Identifiers
PMID: 8840502
Source
Medline
License
Unknown

Abstract

We have isolated two members of the Hsp70 protein family from the yeast Hansenula polymorpha using affinity chromatography. Both proteins were located in the cytoplasm. One of these, designated Hsp72, was inducible in nature (e.g. by heat shock). The second protein (designated Hsc74) was constitutively present. Peptides derived from both Hsp72 and Hsc74 showed sequence homology to the cytosolic Saccharomyces cerevisiae Hsp70s, Ssa1p and Ssa2p. The gene encoding Hsp72 (designated HSA1) was cloned, sequenced and used to construct HSA1 disruption and HSA1 overexpression strains. Comparison of the stress tolerances of these strains with those of wild-type H. polymorpha revealed that HSA1 overexpression negatively affected the tolerance of the cells to killing effects of temperature or ethanol, but enhanced the tolerance to copper and cadmium. The tolerance for other chemicals (arsenite, arsenate, H2O2) or to high osmolarity was unaffected by either deletion or overexpression of HSA1.

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