A proteomic analysis of heat shock proteins from pigeonpea (Cajanus cajan) seed

Résumé

Pigeonpea ( Cajanus cajan L.) is an important grain legume that thrives in harsh agroecosystems, particularly in the semi-arid tropics characterized by high temperatures and recurrent drought. Under such conditions, seed viability may be compromised through thermal denaturation of enzymes and cellular dehydration. Heat shock proteins (HSPs) function as molecular chaperones that protect protein structure and maintain metabolic activity under stress. However, the biochemical basis underlying seed thermo-tolerance in pigeonpea remains poorly understood. This study investigated the occurrence and sequence characteristics of HSPs in mature dry pigeonpea seed. HSPs accounted for 3.14% of the stress-related proteins identified in the seed proteome. Sequence alignment of Hsp70 family proteins revealed highly conserved functional domains and characteristic signature motifs, including the EEVD and EEVK motifs associated with chaperone activity and protein–protein interactions. Conserved regions involved in ATP-dependent regulation, interdomain communication, and co-chaperone binding were also identified, indicating strong structural and functional conservation of Hsp70 proteins in pigeonpea. These findings enhance our understanding of the composition and structural features of heat shock proteins in pigeonpea seed and provide a foundation for future studies investigating their roles in seed longevity, thermo-tolerance, and resilience to prolonged storage and environmental stress.

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