A novel plant peptidyl-prolyl-cis-trans-isomerase (PPIase): cDNA cloning, structural analysis, enzymatic activity and expression

Oshra Blecher, Noa Erel, Isabelle Callebaut, Keren Aviezer, Adina Breiman

Research output: Contribution to journalArticlepeer-review

Abstract

A novel cDNA encoding for a peptidyl-prolyl-cis-trans-isomerase (PPIase) belonging to the FK506-binding protein (FKBP) family was isolated from wheat. It contains an open reading frame of 559 amino acids and it represents the first plant FKBP-PPIase to be cloned. It possesses a unique sequence which is composed of three FKPB-like domains, in addition to a putative tetratricopeptide repeat (TPR) motif and a calmodulin-binding sit. The recombinant FKBP-PPIase expressed in an purified from Escherichia coli exhibits PPIase activity that is efficiently inhibited by the immunosuppressive drugs FK506 and rapamycin. Northern blot analysis showed that wheat FKBP was found mainly in young tissues. Polyclonal antibodies revealed the presence of cross-reacting proteins in embryos, roots and shoots. The unique structural features, the enzymatic activity and the presence of putative isoforms in wheat tissues indicate the possibility of the involvement of wheat PPIase in essential biological functions, similar to other members of the FKBP gene family.

Original languageEnglish
Pages (from-to)493-504
Number of pages12
JournalPlant Molecular Biology
Volume32
Issue number3
DOIs
StatePublished - 1996

Keywords

  • FKBP
  • PPIase
  • cDNA
  • expression
  • wheat

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