The effect of phosphorylation on the salt-tolerance-related functions of the soybean protein PM18, a member of the group-3 LEA protein family

摘要: Enzymatically driven post-translated modifications (PTMs) usually happen within the intrinsically disordered regions of a target protein and can modulate variety functions. Late embryogenesis abundant (LEA) proteins are family plant (IDPs). Despite their important roles in stress response, there is currently limited knowledge on presence functional structural effects phosphorylation LEA proteins. In this study, we identified three sites (Ser90, Tyr136, Thr266) soybean PM18 that belongs to group-3 yeast expression system, increased salt tolerance yeast, further enhanced its protective function. Further analysis revealed Ser90 Tyr136 more than Thr266, these two might work cooperatively regulating resistance function PM18. The circular dichroism showed was aqueous media, did not affect status protein. However, promoted formation helical structure sodium dodecyl sulfate (SDS) or trifluoroethanol (TFE). Furthermore, dedicated vitro experiments, phosphorylated able better protect lactate dehydrogenase (LDH) from inactivation induced by freeze-thaw cycles un- dephosphorylated forms. All data indicate may have regulatory stress-tolerance-related Therefore, studies needed shed light