Carboxylate clamp tetratricopeptide repeat (TPR) domain containing Hsp90 cochaperones in Triticeace: An insight into structural and functional diversification

The molecular chaperones serve as surveillance molecules that mediates regulatory crosstalk between protein folding and degradation pathways under natural and stress conditions. In present study, we focused on the diversification and role of tetratricopeptide repeat (TPR) domain containing Hsp90 cochaperones. These co-chaperone were recognized by the presence of three motifs of TPR with the basic conserved residues often referred to as carboxylate clamp (CC). A total of 213 putative CC-TPRs were found in Triticeace, clustered into 16 groups, amongst which few CC-TPR families such as TPR-RPAP3 and TPR-SMYD were documented. Domain architecture and genomic organization revealed that CC-TPRs are very diverse in nature. Evolutionary analyses showed that CC-TPRs are conserved, stable and ubiquitous in nature. Analysis of available RNA-seq data revealed a high degree of tissue-specific expression of 1-TPR and TaTPR-FKBP family members at various developmental stages. The transcripts of TaCC-TPRs displayed differential expression in two contrasting wheat cultivars under abiotic stress conditions. Complementation and heterologous expression of TaTPR-FKBP5 in yeast conferred abiotic stress tolerance. Together, these results provide a glimpse into the genetic diversity and evolution of CC-TPRs in Triticeace, which would help to better understand of how TPR-domain cochaperones function in plants.