Structure, evolution, and expression analysis of HSP100 genes in Phaseolus vulgaris

Heat shock proteins (HSPs) are integral to plant responses to stress, with HSP100 constituting a significant family involved in protein disaggregation and thermotolerance. This studty investigated the members of HSP100 gene family in Phaseolus vulgaris, Pisum sativum, Glycine max, and Oryza sativa, disclosing variations in gene number (ranging from 8 to 17 members), molecular weight (between 101 and 119 kDa), exon count (ranging 3 to 12), and isoelectric point (from 5.83 to 8.81). Phylogenetic analysis sparated HSP100 family members into four main groups, that each groupshowed specific subcellular localizations (nucleus, chloroplast, mitochondria, and cytoplasm-nucleus). Predictions of phosphorylation sites indicated interspecies variability in members of HSP100 family. Prediction of duplication events in P. vulgaris revealed that segmental duplication events have more occurred in HSP100 family members. Expression analyses disclosed that PHAVU-008g035600g and PHAVU-001g243900g are more linked to responsive to salinity stress. Interaction networks revealed that HSP100s association with SCF ubiquitin ligase components, esterases, CLP proteases, and HSP21, all enriched in ATP-dependent activities. Our findings revealed a deeper understanding of the evolutionary and expression diversity of HSP100 proteins within the plant species.