The Wheat Peptidyl Prolyl Cis-trans-isomerase FKBP77 is Heat Induced and Developmentally Regulated

Overview

Journal Plant Physiol

Specialty Physiology

Date 1999 Feb 10

PMID 9952466

Citations 34

Authors

I Kurek

K Aviezer

N Erel

E Herman

A Breiman

Affiliations

Soon will be listed here.

Abstract

We isolated a cDNA encoding a 568-amino acid, heat-stress-induced peptidyl prolyl isomerase belonging to the FK506-binding-protein (FKBP) family. The open reading frame encodes for a peptidyl prolyl isomerase that possesses three FKBP-12-like domains, a putative tetratricopeptide motif, and a calmodulin-binding domain. Specific antibodies showed that the open reading frame encodes a heat-induced 77-kD protein, the wheat FKBP77 (wFKBP77), which exhibits 84% identity with the wFKBP73 and 42% identity with the human FKBP59. Because of the high similarity in sequence to wFKBP73, wFKBP77 was designated as the heat-induced isoform. The wFKBP77 mRNA steady-state level was 14-fold higher at 37 degreesC than at 25 degreesC. The wFKBP77 transcript abundance was the highest in mature embryos that had imbibed and 2-d-old green shoots exposed to 37 degreesC, and decreased to 6% in 6-d-old green shoots. The transcript level returned to the level detected at 25 degreesC after recovery of the embryos for 90 min at 25 degreesC. We compared wFKBP73 and wFKBP77 with the heat-shock proteins having cognate and heat-stress-induced counterparts.

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