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FEBS Letters
Volume 352, Issue 1, 19 September 1994, Pages 98-103
 
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doi:10.1016/0014-5793(94)00927-9    
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Copyright © 1994 Published by Elsevier B.V.

Purification of FKBP-70, a novel immunophilin from Saccharomyces cerevisiae, and cloning of its structural gene, FPR3

Ute C. Manning-Kriega, Rubén Henríqueza, Florence Cammasa, Patrick Graffa, Samuel Gavériauxa and N.Rao MovvaCorresponding Author Contact Information, a

aSandoz Pharma Ltd., Preclinical Research, Bldg. 386-306, 4002 Basel, Switzerland


Received 18 July 1994; 
revised 11 August 1994. 
Available online 19 October 2001.

Abstract

A novel protein, belonging to the yeast family of FKBPs (FK-binding proteins), FKBP-70, was isolated from Saccharomyces cerevisiae by its interaction with the immunosuppressive agent FK-520. Its structural gene, FPR3, was cloned and the protein expressed and purified from Escherichia coli. This third member of the FKBP family in yeast is homologous to the other FKBPs at its carboxy terminus, showing conserved ligand binding and proline isomerase regions. It is, however,a longer acidic protein with several potential nuclear targeting sequences and a region of homology to nucleolins. Yeast strains deleted for FPR3, as well as a triple deletion mutant of this family of genes, FPR1, FPR2 and FPR3, are viable under normal conditions of growth, indicating that the FPR genes are not essential for life.

Keywords: Immunosuppression; FK506; PPIase; Ascomycin; Yeast; CsA

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Corresponding Author Contact InformationCorresponding author. Fax: (41) (61) 324 2990.

FEBS Letters
Volume 352, Issue 1, 19 September 1994, Pages 98-103
 
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