Abstract：PeaT1 is a protein elicitor from Alternaria tenuissima with a nascent polypeptide associated complex (NAC) domain. In this research, peaT1 was cloned by PCR and ligated to vector pET28a for expression. Then PeaT1 was purified and detected by synchrotron radiation circular dichroism to clarify the relations between heat and its secondary structures. The treatment temperature rose from 4℃, 25℃, 55℃ to 85℃, and then fell from 85℃, 55℃, 25℃ to 4℃. The proportions of α helix and turnel both decreased and then recoverd, the proportion of random coil increased and then recoverd, while the proportion of β sheet kept stable. Further analysis combinded with the structure information of PeaT1 indicated that the NAC domain which formed a homodimer played an essential role in heat resistance. This research illuminated the heat resistance mechanism of PeaT1 and laid the foundation for production and application of PeaT1 as a biological pesticide.
