Two FKBP-related proteins are associated with progesterone receptor complexes

D. F. Smith, B. A. Baggenstoss, Tony Marion, R. A. Rimerman

Research output: Contribution to journalArticle

91 Citations (Scopus)

Abstract

Unactivated steroid receptors are in heterooligomeric complexes that perhaps stabilize a partially folded receptor polypeptide prior to hormone- dependent activation. Hsp90 is a common receptor component and hsp70 is a component of progesterone receptors; both appear to be important as general mediators of protein folding and assembly events. In addition to hsp90, mammalian steroid receptor complexes contain a 52-59-kDa protein that is an FK506-binding immunophilin and has peptidyl-prolyl isomerase activity. Other receptor-associated proteins have been identified but not well- characterized. In the present study, we obtained partial amino acid sequences for two avian progesterone receptor components, p50 and p54. From sequence comparisons with known proteins, they appear to be distinct members of the FKBP family of immunophilins. Six p50 peptide sequences have 80% identity with regions of rabbit FKBP52; seven p54 peptide sequences have 60% identity with rabbit FKBP52. Interaction of p54 with receptor is distinct from p50 in that its binding in vitro is highly sensitive to progesterone or N- ethylmaleimide. An anti-p54 monoclonal antibody was developed that detects a 55-kDa protein in rabbit and human tissues; in a cell-free reconstitution system, the rabbit antigen binds to chicken progesterone receptor along with rFKBP52. While p50 appears to be the chicken homolog of FKBP52, p54 is perhaps a novel member of the FKBP family that, in addition to FKBP52, interacts with progesterone receptor.

Original languageEnglish (US)
Pages (from-to)18365-18371
Number of pages7
JournalJournal of Biological Chemistry
Volume268
Issue number24
StatePublished - Sep 8 1993
Externally publishedYes

Fingerprint

Tacrolimus Binding Proteins
Progesterone Receptors
Immunophilins
Rabbits
Steroid Receptors
Peptides
Chickens
Proteins
Peptidylprolyl Isomerase
Protein folding
Ethylmaleimide
Cell-Free System
Protein Folding
Tacrolimus
Progesterone
Amino Acid Sequence
Chemical activation
Monoclonal Antibodies
Hormones
Tissue

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Smith, D. F., Baggenstoss, B. A., Marion, T., & Rimerman, R. A. (1993). Two FKBP-related proteins are associated with progesterone receptor complexes. Journal of Biological Chemistry, 268(24), 18365-18371.

Two FKBP-related proteins are associated with progesterone receptor complexes. / Smith, D. F.; Baggenstoss, B. A.; Marion, Tony; Rimerman, R. A.

In: Journal of Biological Chemistry, Vol. 268, No. 24, 08.09.1993, p. 18365-18371.

Research output: Contribution to journalArticle

Smith, DF, Baggenstoss, BA, Marion, T & Rimerman, RA 1993, 'Two FKBP-related proteins are associated with progesterone receptor complexes', Journal of Biological Chemistry, vol. 268, no. 24, pp. 18365-18371.
Smith, D. F. ; Baggenstoss, B. A. ; Marion, Tony ; Rimerman, R. A. / Two FKBP-related proteins are associated with progesterone receptor complexes. In: Journal of Biological Chemistry. 1993 ; Vol. 268, No. 24. pp. 18365-18371.
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