Transcriptome and Proteome meta-analysis of tomato chaperone network during ripening

GOYTIA BERTERO VALENTINA; PRATTA GUILLERMO; ARCE DÉBORA PAMELA

Congreso; RAFV Conference 2021 XXXIII Argentinian meeting of Plant Physiology; 2021

Heat Shock Proteins (HSPs) are a super family of chaperones that have been characterized in different organisms. In plants, HSPs participate in the refolding of denatured proteins during physiological processes such as developmental changes and abiotic stress response. The aim of this work was to perform an integrative analysis from a bioinformatic and inferential approach based on protein-protein interaction (PPI) network building in S. lycopersicum cv. Micro-tom during fruit ripening. Expression data publicly available from two independent experiments at transcriptome and proteome levels were included. PPI networks were built using Cytoscape and the MCODE algorithm was applied to identify clusters. Each output cluster was further analyzed with the gene enrichment analysis tool, Fisher’s exact test, p ≤ 0,05 and Benjamini-Hochberg method. GO term enrichment analysis was conducted by the PlanRegMap tool. Our interatomic study allowed us to identify specific networks for each ripening stage of fruit development, evidencing that two clusters during advanced stages were over-represented by HSP families (HSP70 and HSP20), chaperones (Proteasome assembly chaperone) and common protein interactors associated with protein folding, protein synthesis and degradation, and response to stress (GST, ER auxin binding protein, TRP ripening regulated protein). These findings were detected for both levels of analysis: transcriptomic and proteomic, from two independent datasets. Finally, we found that some of these up-regulated chaperones show the presence of HSE motifs in their 5´UTRs. Our combined and inferential bioinformatics approach allowed us to integrate RNA, protein expression and co-expression levels of chaperones involved in cv. Micro-tom during fruit ripening.