Prolyl isomerases in yeast.

Published online

Journal Article (Review)

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.

Full Text

Duke Authors

Cited Authors

  • Arevalo-Rodriguez, M; Wu, X; Hanes, SD; Heitman, J

Published Date

  • September 1, 2004

Published In

Volume / Issue

  • 9 /

Start / End Page

  • 2420 - 2446

PubMed ID

  • 15353296

Pubmed Central ID

  • 15353296

International Standard Serial Number (ISSN)

  • 1093-9946

Digital Object Identifier (DOI)

  • 10.2741/1405

Language

  • eng

Conference Location

  • United States