The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase

John J. Siekierka, Gregory Wiederrecht, Heidi Greulich, David Boulton, Shirley H.Y. Hung, John Cryan, Paul J. Hodges, Nolan H. Sigal

Research output: Contribution to journalArticlepeer-review

129 Scopus citations

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 possesses 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.

Original languageEnglish
Pages (from-to)21011-21015
Number of pages5
JournalJournal of Biological Chemistry
Volume265
Issue number34
StatePublished - 5 Dec 1990

Fingerprint

Dive into the research topics of 'The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase'. Together they form a unique fingerprint.

Cite this