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Saccharomyces cerevisiae contains a homolog of human fkbp‐13, a membrane‐associated fk506/rapamycin binding protein
Author(s) -
Partaledis Judith A.,
Fleming Mark A.,
Harding Matthew W.,
Berlin Vivian
Publication year - 1992
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.320080812
Subject(s) - fkbp , biology , saccharomyces cerevisiae , amino acid , biochemistry , binding protein , peptide sequence , yeast , microbiology and biotechnology , gene
FKB2 encodes a homolog of human FKBP‐13, a membrane‐associated binding protein for the immunosuppressants FK506 and rapamycin. FKB2 is located on the right arm of chromosome IV and contains an open reading frame of 135 amino acids, of which the first 17 residues comprise a putative hydrophobic leader peptide. Yeast FKBP‐13 is homologous to human FKBP‐13 (52% amino acid identity) and to FKBP‐12, the major cytosolic receptor for FK506. In the alignment of FKBP‐13 and FKBP‐12 sequences, there are 28 invariant residues. Among these conserved residues are those that comprise the drug binding and peptidyl‐prolyl cis ‐ trans isomerase active site of FKBP‐12. The phylogenetic conservation of the FKBP family suggests that the proteins are involved in a basic cellular function.