Evolution of the 12 kDa FK506‐binding protein gene

Abstract

Background information. The FKBPs (FK506-binding proteins) belong to a ubiquitous family of proteins that are found in a wide range of taxonomic groups. These proteins participate in a variety of pathways, including protein folding, down-regulation of T-cell activation and inhibition of cell-cycle progression.Results. A cDNA encoding the 12 kDa FKBP gene orthologue (FKBP12) in Bombyx mori was been isolated from both Bm-5 cultured cells and silk-gland tissue. Using the FKBP12 cDNA in combination with the B. mori 6× wholegenome shotgun database, we were able to identify the FKBP12 gene, as well as the positions of its intron-exon junctions.Conclusions. FKBP12 exon sizes and intronic positions are highly conserved among FKBP12 orthologues in 24 diverse genomes. Comparison of 41 FKBP12 genes revealed several intronic insertion and deletion events throughout evolution. In addition, paralogous FKBP12 isoforms were identified in all 12 vertebrate genomes. Both structural and phylogenetics analyses suggest that the isoforms may be evolving independently, possibly due to the distinct functional roles played by each paralogue.

Identifying genes that interact with Drosophila presenilin and amyloid precursor protein

“…Overexpression of Psn results in the accumulation of protein aggregates (data not shown), and has previously been shown to increase apoptosis levels, possibly due to dominant-negative effects . This may explain why a large number of stress response genes, cell cycling components, and cell death factors were identified as Psn modifiers, including CycE, ex, Hsp83, Ras85D, and thread (Huang et al, 2005;Maitra et al, 2006;Polesello and Tapon, 2007;Saucedo and Edgar, 2007;Somarelli and Herrera, 2007). For example, a reduction in the levels of thread, a gene implicated in apoptosis, would be expected to suppress the Psn-dependent phenotypes simply by reducing the overall levels of cell death in the wing or notum.…”

Genome-wide analysis and environmental response profiling of the FK506-binding protein gene family in maize (Zea mays L.)

“…5.1.2.8) are well known receptors of the immunosuppressive drug FK506 and therefore are also referred to as immunophilins (Bierer et al, 1990;Harding et al, 1989;Siekierka et al, 1989). Each FKBP is composed of at least one FK506-binding domain (FKBd), a conserved peptide sequence of about 110 amino acids also known as FKBP12 (Galat, 2000;Somarelli and Herrera, 2007). Singledomain (low-molecular weight) FKBPs consist essentially of the FKBd, while multidomain (high-molecular weight) FKBPs contain up to three FKBds, along with tetratricopeptide repeat (TPR), coiled-coil domain (CCD) or C-terminal calmodulin-binding domains (CaM-BDs) for protein-protein interactions or recognition, or for the assembly of multi-protein complexes (Geisler and Bailly, 2007;Nigam et al, 2008).…”

Genome wide analysis ofCyclophilingene family from rice and Arabidopsis and its comparison with yeast

“…The Cyclophilin gene sequences were verified on the basis of presence of conserved PPIase motif by carrying out domain scan using Prosite from the Expasy resource portal (http://prosite.expasy.org/). 57,58 The genes that co-expressed with Arabidopsis Cyclophilins were predicted using ATTED-II (http://atted.jp/). The information regarding the molecular weight, pI and number of amino acid of Arabidopsis and rice cyclophilin proteins was retrieved from (TAIR) database (http:// www.arabidopsis.org/) 59 and from http://rice.plant biology.msu.…”