IMR Press / FBL / Volume 9 / Issue 4 / DOI: 10.2741/1405

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
Prolyl isomerases in yeast
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1 Departments of Molecular Genetics and Microbiology, Howard Hughes Medical Institute, Duke University Medical Center, Durham, NC 27710, USA
2 Departments of Pharmacology and Cancer Biology, and Medicine, Howard Hughes Medical Institute, Duke University Medical Center, Durham, NC 27710, USA
3 Molecular Genetics Program, Wadsworth Center, New York State Department of Health, and Department of Biomedical Sciences, School of Public Health, State University of New York, Albany, NY 12208, USA
Academic Editor:Kun Lu
Front. Biosci. (Landmark Ed) 2004, 9(4), 2420–2446; https://doi.org/10.2741/1405
Published: 1 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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