I. Kurek et al., Isolation and characterization of the wheat prolyl isomerase FK506-bindingprotein (FKBP) 73 promoter, PLANT MOL B, 42(3), 2000, pp. 489-497
The wheat FK506-binding protein (FKBP) 73 is a member of the peptidyl proly
l cis-trans isomerase gene family, which catalyses the interconversion betw
een the cis and trans forms of the peptide bond preceding proline residues
in proteins. A 3.5 kb sequence 5' upstream of the ATG codon of the wheat FK
BP73 was isolated from a wheat genomic library, and characterized by deleti
on analysis and transient expression in wheat embryos. The 1517 bp fragment
is referred to as the full promoter due to the maximal activity of the fus
ed luciferase reporter gene. Sequence analysis revealed the presence of thr
ee abscisic acid (ABA)-responsive elements (ABREs) proximal to coupling ele
ments (CE1-like), a putative lectin box, two putative binding sites for the
myb transcription factor and a 36 bp fragment which exhibits 100% identity
to the pSau3A9 clone located in the centromeric region of wheat chromosome
s. In a transient expression assay the promoter preserved the tissue specif
icity described in vivo, namely it is expressed only in germinating embryos
and young shoots. The promoter was induced 1.9-fold by ABA, the minimal pr
omoter was designated at -221 and the TATA box located at -137. The inducib
ility by ABA and the expression during germination may indicate that FKBP73
belongs to the group of genes induced by ABA upon germination.