FKB1 encodes a nonessential FK 506-binding protein in Saccharomyces cerevisiae and contains regions suggesting homology to the cyclophilins

G. Wiederrecht, L. Brizuela, K. Elliston, N. H. Sigal, John Siekierka

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Abstract

FK 506, a powerful immunosuppressant that blocks allograft rejection by preventing T-cell activation, binds to an 11-kDa protein called the FK 506-binding protein (FKBP). Like cyclophilin, a cytosolic protein that binds another immunosuppressant, cyclosporin A, FKBP possesses peptidylprolyl cis-trans isomerase activity. We have isolated a genomic clone encoding the yeast FKBP (FKB1). The gene encodes a protein of 114 amino acids having a calculated M(r) of 12,158. Disruption of the gene shows that FKB1 is not essential for growth. A search of translated nucleic acid data bases revealed bacterial FKBP homologs in Neisseria meningiditis and Pseudomonas aeruginosa. Comparison of the conserved amino acids in FKBP homologs with the conserved amino acids in the cyclophilins has revealed a region of similarity that we speculate to be a homologous domain related to the functional similarities of the two proteins.

Original languageEnglish
Pages (from-to)1029-1033
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume88
Issue number3
DOIs
StatePublished - 21 Feb 1991

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Tacrolimus Binding Proteins
Cyclophilins
Saccharomyces cerevisiae
Immunosuppressive Agents
Amino Acids
cis-trans-Isomerases
Proteins
Peptidylprolyl Isomerase
Neisseria
Fungal Proteins
Bacterial Proteins
Tacrolimus
Pseudomonas aeruginosa
Nucleic Acids
Cyclosporine
Genes
Allografts
Clone Cells
Databases
T-Lymphocytes

Cite this

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title = "FKB1 encodes a nonessential FK 506-binding protein in Saccharomyces cerevisiae and contains regions suggesting homology to the cyclophilins",
abstract = "FK 506, a powerful immunosuppressant that blocks allograft rejection by preventing T-cell activation, binds to an 11-kDa protein called the FK 506-binding protein (FKBP). Like cyclophilin, a cytosolic protein that binds another immunosuppressant, cyclosporin A, FKBP possesses peptidylprolyl cis-trans isomerase activity. We have isolated a genomic clone encoding the yeast FKBP (FKB1). The gene encodes a protein of 114 amino acids having a calculated M(r) of 12,158. Disruption of the gene shows that FKB1 is not essential for growth. A search of translated nucleic acid data bases revealed bacterial FKBP homologs in Neisseria meningiditis and Pseudomonas aeruginosa. Comparison of the conserved amino acids in FKBP homologs with the conserved amino acids in the cyclophilins has revealed a region of similarity that we speculate to be a homologous domain related to the functional similarities of the two proteins.",
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FKB1 encodes a nonessential FK 506-binding protein in Saccharomyces cerevisiae and contains regions suggesting homology to the cyclophilins. / Wiederrecht, G.; Brizuela, L.; Elliston, K.; Sigal, N. H.; Siekierka, John.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 88, No. 3, 21.02.1991, p. 1029-1033.

Research output: Contribution to journalArticleResearchpeer-review

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AU - Wiederrecht, G.

AU - Brizuela, L.

AU - Elliston, K.

AU - Sigal, N. H.

AU - Siekierka, John

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AB - FK 506, a powerful immunosuppressant that blocks allograft rejection by preventing T-cell activation, binds to an 11-kDa protein called the FK 506-binding protein (FKBP). Like cyclophilin, a cytosolic protein that binds another immunosuppressant, cyclosporin A, FKBP possesses peptidylprolyl cis-trans isomerase activity. We have isolated a genomic clone encoding the yeast FKBP (FKB1). The gene encodes a protein of 114 amino acids having a calculated M(r) of 12,158. Disruption of the gene shows that FKB1 is not essential for growth. A search of translated nucleic acid data bases revealed bacterial FKBP homologs in Neisseria meningiditis and Pseudomonas aeruginosa. Comparison of the conserved amino acids in FKBP homologs with the conserved amino acids in the cyclophilins has revealed a region of similarity that we speculate to be a homologous domain related to the functional similarities of the two proteins.

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