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

John Siekierka, G. Wiederrecht, H. Greulich, D. Boulton, S. H.Y. Hung, J. Cryan, P. J. Hodges, N. H. Sigal

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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.

Original languageEnglish
Pages (from-to)21011-21015
Number of pages5
JournalJournal of Biological Chemistry
Volume265
Issue number34
StatePublished - 1 Dec 1990

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Tacrolimus Binding Proteins
Peptidylprolyl Isomerase
Tacrolimus
Immunosuppressive Agents
Carrier Proteins
T-cells
Proteins
T-Lymphocytes
Thymus
Amino Acid Sequence Homology
Eukaryotic Cells
Yeast
Thymus Gland
Saccharomyces cerevisiae
Conformations
Molecular Weight
Molecular weight
Cells
Amino Acids
Cell Line

Cite this

Siekierka, J., Wiederrecht, G., Greulich, H., Boulton, D., Hung, S. H. Y., Cryan, J., ... Sigal, N. H. (1990). The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase. Journal of Biological Chemistry, 265(34), 21011-21015.
Siekierka, John ; Wiederrecht, G. ; Greulich, H. ; Boulton, D. ; Hung, S. H.Y. ; Cryan, J. ; Hodges, P. J. ; Sigal, N. H. / The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase. In: Journal of Biological Chemistry. 1990 ; Vol. 265, No. 34. pp. 21011-21015.
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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.",
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Siekierka, J, Wiederrecht, G, Greulich, H, Boulton, D, Hung, SHY, Cryan, J, Hodges, PJ & Sigal, NH 1990, 'The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase', Journal of Biological Chemistry, vol. 265, no. 34, pp. 21011-21015.

The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase. / Siekierka, John; Wiederrecht, G.; Greulich, H.; Boulton, D.; Hung, S. H.Y.; Cryan, J.; Hodges, P. J.; Sigal, N. H.

In: Journal of Biological Chemistry, Vol. 265, No. 34, 01.12.1990, p. 21011-21015.

Research output: Contribution to journalArticleResearchpeer-review

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AU - Siekierka, John

AU - Wiederrecht, G.

AU - Greulich, H.

AU - Boulton, D.

AU - Hung, S. H.Y.

AU - Cryan, J.

AU - Hodges, P. J.

AU - Sigal, N. H.

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AB - 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.

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