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Purification of FKBP‐70, a novel immunophilin from Saccharomyces cerevisiae , and cloning of its structural gene, FPR3
Author(s) -
Manning-Krieg Ute C.,
Henríquez Rubén,
Cammas Florence,
Graff Patrick,
Gavériaux Samuel,
Movva N.Rao
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00927-9
Subject(s) - fkbp , saccharomyces cerevisiae , yeast , biology , mutant , prolyl isomerase , gene , biochemistry , peptidylprolyl isomerase , escherichia coli , cloning (programming) , genetics , isomerase , pin1 , computer science , programming language
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.