cDNA Cloning of a Putative Protochoradate FK506-Binding Protein

Z. Pancer, H. Gershon, B. Rinkevich

Research output: Contribution to journalArticlepeer-review


A tunicate (Botryllus schlosseri) cDNA library was screened with a microsatellite probe. Five positive clones were sequenced, each with a 5′ truncated microsatellite. One (Bs.6) revealed striking similarity to FK506 and rapamycin-binding proteins (FKBPs). Clone Bs.6 is 500 base pairs long and encodes for a putative protein of 134 amino acids. The predicted protein features the two FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase) signatures and an endoplasmic reticulum retention signal. This protochordate protein is substantially similar to 12-13 kDa FKBPs, most remarkably to one of the receptors that had been proposed to mediate the immunosuppressive actions of FK506, the human FKBP-13 (62% amino acid identity and 74% similarity).

Original languageEnglish
Pages (from-to)973-977
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - 15 Dec 1993
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry
  • Cell Biology


Dive into the research topics of 'cDNA Cloning of a Putative Protochoradate FK506-Binding Protein'. Together they form a unique fingerprint.

Cite this