Genome-wide analysis of immunophilin FKBP genes and expression patterns in Zea mays

• Published in: Genetics and molecular research Vol. 11; no. 2; pp. 1690 - 1700
• Main Authors: Wang, W-W, Ma, Q, Xiang, Y, Zhu, S-W, Cheng, B-J
• Format: Journal Article
• Language: English
• Published: Brazil 01.01.2012
• Subjects: Computer applications; Gene Duplication - genetics; Oryza sativa; Phylogeny; Plant Proteins - genetics; Reverse Transcriptase Polymerase Chain Reaction; Tacrolimus Binding Proteins - classification; Tacrolimus Binding Proteins - genetics; Zea mays - genetics
• ISSN: 1676-5680; 1676-5680
• DOI: 10.4238/2012.June.25.2

The receptors for the immunosuppression drugs FK506 and rapamycin are called FKBPs (FK506-binding proteins). FKBPs comprise a large family; they are found in many species, including bacteria, fungi, animals, and plants. As a class of peptidyl-prolyl cis-trans isomerase enzymes, the FKBP genes have been the focus of recent studies on plant stress tolerance and immunology. We identified and analyzed gene families encoding these proteins in maize using computational and molecular biology approaches. Thirty genes were found to encode putative FKBPs according to their FK506-binding domain. The FKBP genes can be classified into single domain and multiple domain members based on the number of the domains. By analysis of the physical locations, the 30 FKBP genes were found to be widely distributed on 10 chromosomes. After analysis of the FKBP phylogenetic tree in the maize genome, we found that the 30 genes revealed two major clades. Gene duplication played a major role in the evolution of FKBP genes, which suggests that the FKBP genes in maize have a pattern significantly different from that of these genes in rice. Based on semi-quantitative RT-PCR, we found that the 30 FKBPs were expressed differently in various tissues in maize, which suggests that FKBP genes play different roles in each tissue. Several FKBPs were expressed at higher levels in roots, indicating that these genes in maize may have similar or overlapping functions.