Prolyl isomerases in yeast.
Journal Article (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
International Standard Serial Number (ISSN)
- 1093-9946
Digital Object Identifier (DOI)
- 10.2741/1405
Language
- eng
Conference Location
- United States