Prolyl isomerases in yeast

Front Biosci. 2004 Sep 1;9:2420-46. doi: 10.2741/1405.

Abstract

Prolyl isomerases are enzymes that catalyze cis-trans isomerization of peptidyl-prolyl bonds and span three structurally unrelated protein families: the cyclophilins, FKBPs, and parvulins. The genome of the budding yeast Saccharomyces cerevisiae encodes eight different cyclophilins (Cpr1 to Cpr8), four FKBPs (Fpr1 to Fpr4), and a single parvulin (Ess1). Remarkably, two of these proteins, cyclophilin A and FKBP12, are conserved from yeast to humans and mediate virtually all of the intracellular actions of the immunosuppressive antifungal drugs cyclosporin A, FK506, and rapamycin. The study of prolyl isomerases in S. cerevisiae has proven invaluable to understand the elusive functions of these proteins, and continues to provide new insights into their diverse cellular roles. Here we review the current state of knowledge about prolyl-isomerases in this model organism.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Conserved Sequence
  • Cyclophilin A / chemistry
  • Cyclophilins / metabolism*
  • Cyclosporine / pharmacology
  • Gene Expression Regulation, Fungal*
  • Genome, Fungal*
  • Humans
  • Mitosis
  • Peptidylprolyl Isomerase / chemistry
  • Peptidylprolyl Isomerase / physiology*
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae / metabolism
  • Sirolimus / pharmacology
  • Species Specificity
  • Tacrolimus / pharmacology
  • Tacrolimus Binding Protein 1A / metabolism

Substances

  • Cyclosporine
  • Cyclophilin A
  • Cyclophilins
  • Tacrolimus Binding Protein 1A
  • Peptidylprolyl Isomerase
  • Sirolimus
  • Tacrolimus