Prolyl isomerases in yeast.
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.
Arevalo-Rodriguez
Miguel
M
Department of Molecular Genetics and Microbiology, Howard Hughes Medical Institute, Duke University Medical Center, Durham, NC 27710, USA.
Wu
Xiaoyun
X
Hanes
Steven D
SD
Heitman
Joseph
J
D017124:Conserved Sequence; D021984:Cyclophilin A / Q000737:chemistry; D021983:Cyclophilins / Q000378:metabolism*; D016572:Cyclosporine / Q000494:pharmacology; D015966:Gene Expression Regulation, Fungal; D016681:Genome, Fungal; D006801:Humans; D008938:Mitosis; D019696:Peptidylprolyl Isomerase / Q000737:chemistry / Q000502:physiology*; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000378:metabolism; D020123:Sirolimus / Q000494:pharmacology; D013045:Species Specificity; D016559:Tacrolimus / Q000494:pharmacology; D022061:Tacrolimus Binding Protein 1A / Q000378:metabolism
D016572:Cyclosporine; D021984:Cyclophilin A; D021983:Cyclophilins; D022061:Tacrolimus Binding Protein 1A; D019696:Peptidylprolyl Isomerase; D020123:Sirolimus; D016559:Tacrolimus