Related Experiment Video
Updated: Aug 22, 2026

Budding Yeast Protein Extraction and Purification for the Study of Function, Interactions, and Post-translational Modifications
Published on: October 30, 2013
Prolyl isomerases in yeast
Miguel Arevalo-Rodriguez1, Xiaoyun Wu, Steven D Hanes
1Department of Molecular Genetics and Microbiology, Howard Hughes Medical Institute, Duke University Medical Center, Durham, NC 27710, USA.
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.
Related Concept Videos
Yeast Signaling
Eukaryotic RNA Polymerases
All three eukaryotic RNAPs require specific transcription factors, of which the...
Bioreactor Controls-III
Replication in Prokaryotes
Many Proteins Work Together to Replicate the Chromosome
Replication is coordinated and carried out by a host of specialized...
Replication in Prokaryotes
Replication in Prokaryotes

