Functional analysis of the yeast 40 kDa cyclophilin Cyp40 and its role for viability and steroid receptor regulation

Biol Chem. 1997 May;378(5):381-91. doi: 10.1515/bchm.1997.378.5.381.

Abstract

We have identified and characterized a homolog of the 40 kDa cyclophilins in the budding yeast Saccharomyces cerevisiae. At the amino acid level, this novel yeast cyclophilin, termed Cyp40, is 47% identical to human cyclophilin-40. Recombinant Cyp40 produced in bacteria has a peptidyl-prolyl cis-trans isomerase activity with a catalytic efficiency (k[cat]/K[m]) of 0.5 x 10(6)M(-1)s(-1), which can be inhibited by cyclosporin A with an IC50 value of 60nM. Using a polyclonal antibody against Cyp40 we have found that Cyp40 is predominantly cytoplasmic, and that its expression is induced 3-4-fold by heat shock. Moreover, Cyp40 can be coprecipitated from yeast extracts with the cytosolic molecular chaperone Hsp90. Surprisingly, a Cyp40-deficient yeast strain is fully viable at normal and elevated temperatures. Cyp40 is also dispensable for normal regulation of vertebrate steroid receptors in yeast. While other immunophilins could conceivably compensate a Cyp40 defect, our results are compatible with the notion that immunophilins may be fortuitous partners in the biochemically established steroid receptor-Hsp90 complex.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Isomerases / chemistry
  • Amino Acid Isomerases / genetics
  • Amino Acid Isomerases / physiology*
  • Amino Acid Sequence
  • Base Sequence
  • Binding Sites
  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics
  • Carrier Proteins / physiology*
  • Chromatography, Affinity
  • Cloning, Molecular
  • Cyclosporine / pharmacology
  • Cytoplasm / enzymology
  • Endodeoxyribonucleases / chemistry
  • Endodeoxyribonucleases / genetics
  • Endodeoxyribonucleases / physiology*
  • Fungal Proteins / metabolism
  • HSP90 Heat-Shock Proteins
  • Heat-Shock Proteins / metabolism
  • Humans
  • Immunosuppressive Agents / pharmacology
  • Molecular Sequence Data
  • Molecular Weight
  • Peptidylprolyl Isomerase
  • Receptors, Steroid / physiology*
  • Recombinant Proteins / metabolism
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae Proteins
  • Stereoisomerism
  • beta-Galactosidase / metabolism

Substances

  • Carrier Proteins
  • Fungal Proteins
  • HSP82 protein, S cerevisiae
  • HSP90 Heat-Shock Proteins
  • Heat-Shock Proteins
  • Immunosuppressive Agents
  • Receptors, Steroid
  • Recombinant Proteins
  • Saccharomyces cerevisiae Proteins
  • Cyclosporine
  • Endodeoxyribonucleases
  • beta-Galactosidase
  • Amino Acid Isomerases
  • Peptidylprolyl Isomerase

Associated data

  • GENBANK/U48867
  • GENBANK/U48868