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 <i>CsHSP70</i> genes present and verified in <i>Camelina sativa</i>, 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 <i>CsHSP70</i> 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 <i>CsHsp70</i>. An analysis of transcriptome data exposed to cold, drought, salinity, and cadmium stress demonstrated the varied expression profiles of <i>CsHsp70</i> genes. The expression levels of <i>CsHSP70</i> 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 <i>CsHsp70-60</i>, -<i>52</i>, and -<i>13</i> were up-regulated and <i>CsHsp70-03</i>, -<i>58</i>, and -<i>09</i> showed down-regulation in response to salinity. Furthermore, <i>CsHsp70</i> 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.