Uc. Manningkrieg et al., PURIFICATION OF FKBP-70, A NOVEL IMMUNOPHILIN FROM SACCHAROMYCES-CEREVISIAE, AND CLONING OF ITS STRUCTURAL GENE, FPR3, FEBS letters, 352(1), 1994, pp. 98-103
A novel protein, belonging to the yeast family of FKBPs (FK-binding pr
oteins), FKBP-70, was isolated from Saccharomyces cerevisiae by its in
teraction with the immunosuppressive agent FK-520. Its structural gene
, FPR3, was cloned and the protein expressed and purified from Escheri
chia 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 regi
on of homology to nucleolins. Yeast strains deleted for FPR3, as well
as a triple deletion mutant of this family of genes, FPR1, FPR2 and FP
R3, are viable under normal conditions of growth, indicating that the
FPR genes are not essential for life.