Abstract: In order to study the role of AhpC of Thermoanaerobacter tengcongensis in thermophilic adaptation, the prokaryotic expression vector pET-28a :: ahpC was constructed and expressed in Escherichia coli BL21(DE3) using PCR to amplify the ahpC of T. tengcongensis. mRNA expression levels of the ahpC at 50 ℃, 60 ℃, 75 ℃ and 80 ℃ were analyzed by quantitative real time polymerase chain reaction (qRT-PCR). The mass of AhpC was 26 ku, which was mainly in soluble form. qRT-PCR analysis shown that the mRNA expression of ahpC was increased with the increase of temperature. Bioinformatics analysis showed that the ahpC gene was 663 bp in length and encoded 220 amino acids. The contents of Glu (E) and Lys (K) were higher than those of normal bacteria. It is predicted that 29.1% of the amino acids in the secondary structure of the protein are involved in the formation of α-helix structure. The tertiary structure of the AhpC in Thermoanaerobacter tengcongensis is significantly more compact than those of E. coli and Listeria monocytogenes. The results of this study have a certain help for the study of thermophilic adaptation of Thermoanaerobacter tengcongensis.

Key words: Thermoanaerobacter tengcongensis, AhpC, thermophilic adaptation