Insights into the Heat Shock Protein 70 (Hsp70) Family in Camelina sativa and Its Roles in Response to Salt Stress

Hsp70s, a group of heat shock proteins, are ancient proteins that play a crucial part in maintaining the stability of cells when faced with various internal and external stresses. In this research, there are 72 CsHSP70 genes present and verified in Camelina sativa, all of which exhibit a wide range of physicochemical characteristics. Through evolutionary analysis, the Hsp70 family was categorized into five primary groups, and numerous segmental duplications were anticipated among the CsHSP70 genes. The GO enrichment analysis of co-expression network elements revealed a significant association between key signaling terms, such as phosphorelay signal transduction, and MAPK cascade with the function of CsHsp70. An analysis of transcriptome data exposed to cold, drought, salinity, and cadmium stress demonstrated the varied expression profiles of CsHsp70 genes. The expression levels of CsHSP70 genes varied across various organs and stages of development in camelina, although some of them illustrated tissue-specific expression. qRT-PCR analysis further disclosed that CsHsp70-60, -52, and -13 were up-regulated and CsHsp70-03, -58, and -09 showed down-regulation in response to salinity. Furthermore, CsHsp70 genes are categorized as late-responsive elements to salinity stress. Through docking analysis, the current research revealed that CsHsp70 proteins interacted with ABA, BR, and MeJA.