The Cytosolic-Binding Protein for the Immunosuppressant FK-506 Is Both a Ubiquitous and Highly Conserved Peptidyl-Prolyl Cis-Trans Isomerase
Document Type
Article
Publication Date
12-1-1990
Abstract
We have recently isolated an abundant cytosolic protein from human T-cells which specifically binds the immunosuppressive agent, FK-506. The FK-506-binding protein (FKBP) is a member of a novel class of proteins possessing peptidyl-prolyl cis-trans isomerase activity. These proteins are believed to play an important role in accelerating the rate at which proteins fold into their native conformations. In the present study, we demonstrate that FKBP is not a lymphoid-specific protein, but is widely distributed and phylogenically conserved. FKBP, purified from three sources (a human T-lymphocyte cell line JURKAT, bovine calf thymus, and Saccharomyces cerevisiae) exhibit identical molecular weights, immunological cross-reactivities, and a high degree of NH2-terminal amino acid sequence homology. In addition, FKBP from all sources possessess peptidyl-prolyl cis-trans isomerase activity which can be specifically inhibited by FK-506. We conclude that FKBP may serve an important biological function in all eukaryotic cells.
Montclair State University Digital Commons Citation
Siekierka, John; Wiederrecht, Gregory; Greulich, Heidi; Boulton, D.; Hung, Shirley H.Y.; Cryan, John G.; Hodges, P. J.; and Sigal, Nolan H., "The Cytosolic-Binding Protein for the Immunosuppressant FK-506 Is Both a Ubiquitous and Highly Conserved Peptidyl-Prolyl Cis-Trans Isomerase" (1990). Department of Chemistry and Biochemistry Faculty Scholarship and Creative Works. 472.
https://digitalcommons.montclair.edu/chem-biochem-facpubs/472