Peattie, Debra A.;
Harding, Matthew W.;
Fleming, Mark A.;
DeCenzo, Maureen T.;
Lippke, Judith A.;
Livingston, David J.;
Benasutti, Matt
Expression and Characterization of Human FKBP52, an Immunophilin that Associates with the 90-kDa Heat Shock Protein and is a Component of Steroid Receptor Complexes
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Media type:
E-Article
Title:
Expression and Characterization of Human FKBP52, an Immunophilin that Associates with the 90-kDa Heat Shock Protein and is a Component of Steroid Receptor Complexes
Contributor:
Peattie, Debra A.;
Harding, Matthew W.;
Fleming, Mark A.;
DeCenzo, Maureen T.;
Lippke, Judith A.;
Livingston, David J.;
Benasutti, Matt
Published:
National Academy of Sciences of the United States of America, 1992
Published in:
Proceedings of the National Academy of Sciences of the United States of America, 89 (1992) 22, Seite 10974-10978
Language:
English
ISSN:
0027-8424
Origination:
Footnote:
Description:
<p>Using an FK506 affinity column to identify mammalian immunosuppressant-binding proteins, we identified an immunophilin with an apparent M<sub>r</sub>≈ 55,000, which we have named FKBP52. We used chemically determined peptide sequence and a computerized algorithm to search GenPept, the translated GenBank data base, and identified two cDNAs likely to encode the murine FKBP52 homolog. We amplified a murine cDNA fragment, used it to select a human FKBP52 (hFKBP52) cDNA clone, and then used the clone to deduce the hFKBP52 sequence (calculated M<sub>r</sub>51,810) and to express hFKBP52 in Escherichia coli. Recombinant hFKBP52 has peptidyl-prolyl cis-trans isomerase activity that is inhibited by FK506 and rapamycin and an FKBP12-like consensus sequence that probably defines the immunosuppressant-binding site. FKBP52 is apparently common to several vertebrate species and associates with the 90-kDa heat shock protein (hsp90) in untransformed mammalian steroid receptor complexes. The putative immunosuppressant-binding site is probably distinct from the hsp90-binding site, and we predict that FKBP52 has different structural domains to accommodate these functions. hFKBP52 contains 12 protein kinase phosphorylation-site motifs and a potential calmodulin-binding site, implying that posttranslational phosphorylation could generate multiple isoforms of the protein and that calmodulin and intracellular Ca<sup>2+</sup>levels could affect FKBP52 function. FKBP52 transcripts are present in a variety of human tissues and could vary in abundance and/or stability.</p>