The FKBP protein family has prolyl isomerase activity and is related in function to cyclophilins. FKBPs are known to be involved in many biological processes including hormone signaling, plant growth, and stress responses through a chaperone or an isomerization of proline residues during protein folding. The availability of complete peach genome sequences allowed the identification of 21 FKBP genes by HMMER and BLAST analyses. Scaffold locations of these FKBP genes in the peach genome were determined and the protein domain and motif organization of peach FKBPs were analyzed. The phylogenetic relationships between peach FKBPs were also assessed. The expression profiles of peach FKBP gene results revealed that most peach FKBPs were expressed in all tissues, while a few peach FKBPs were specifically expressed in some of the tissues. This data could contribute to better understanding of the complex regulation of the peach FKBP gene family, and also provide valuable information for further research in peach functional genomics.
Keywords: Bioinformatics analysis; CDS; CaM-BDs; ER; FK506-binding domain; FK506-binding proteins; FKBPs; FKBd; HSP90; MD; PPIase; Peach; RT-PCR; SD; Sequence express analysis; TPR; calmodulin-binding domains; coding sequence; endoplasmic reticulum; heat streak protein 90; multidomain; peptidyl-prolylcis-trans isomerase; qRT-PCR; quantitative real-time PCR; semi-quantitative reverse transcription PCR; single-domain; tetratricopeptide repeat.
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