The Wheat Peptidyl Prolyl
cis-trans-Isomerase FKBP77 Is Heat
Induced and Developmentally Regulated1
Isaac Kurek,
Keren Aviezer,
Noa Erel,
Eliot Herman, and
Adina Breiman*
The George S. Wise Faculty of Life Sciences, Department of Plant
Sciences, Tel Aviv University, Tel Aviv, Israel 69978 (I.K., K.A.,
N.E., A.B.); and Climate Stress Laboratory, United States Department of
Agriculture-Agricultural Research Service, Beltsville, Maryland 20705 (E.H.)
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°C than at 25°C. The wFKBP77 transcript abundance was the highest
in mature embryos that had imbibed and 2-d-old green shoots exposed to
37°C, and decreased to 6% in 6-d-old green shoots. The transcript
level returned to the level detected at 25°C after recovery of the
embryos for 90 min at 25°C. We compared wFKBP73 and wFKBP77 with the
heat-shock proteins having cognate and heat-stress-induced
counterparts.
1
This work was supported by a grant from the
Israeli Academy of Science to A.B.
*
Corresponding author; e-mail adina{at}ccsg.tau.ac.il; fax
972-3-640-9380.
Plant Physiol. (1999) 119: 693-704
Copyright Clearance Center: 0032-0889/99/119//12
© 1999 American Society of Plant Physiologists
