Open Access
Article
Prolyl isomerases in yeast
Miguel Arevalo-Rodriguez1,Xiaoyun Wu1,Steven D Hanes1,Joseph Heitman1
1
Department of Molecular Genetics and Microbiology, Howard Hughes Medical Institute, Duke University Medical Center, Durham, NC 27710, USA
DOI: 10.2741/1405 Volume 9 Issue 4, pp.2420-2446
Published: 01 September 2004
(This article belongs to the Special Issue Prolyl isomerases in cell signaling and diseases)
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.

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Miguel Arevalo-Rodriguez, Xiaoyun Wu, Steven D Hanes, Joseph Heitman. Prolyl isomerases in yeast. Frontiers in Bioscience-Landmark. 2004. 9(4); 2420-2446.