Abstract

ATP synthase is a key enzyme in the cellular energy metabolism. In the present study, cDNA of ATP synthase subunit from Sinonovacula constricta (ScATPase) was isolated and characterized by cDNA library and RACE appraoaches. The full-length cDNA of ScATPase was of 737 bp, consisting of a 5'-untranslated region (UTR) of 48 bp, a 3'-UTR of 248 bp and a complete open-reading frame of 441 bp, encoding a polypeptide of 146 amino acid residues with preidicted molecular mass of 15.4 kDa and theoretical isoelectric point of 9.33. BLASTp and phylogenentic analysis revealed that, the deduced amino acid of ScATPase shared higher identity with the ATP synthase subunit C subunit from other species, indicating it should be a novel member of ATPase C family. Quantitative real-time polymerase chain reaction (RT-PCR) analysis indicated that, the expression of ScATPase could be induced by the thermal stress in three different tissues. These results strongly suggest that, ScATPase was an acute protein involved in temperature challenge in S. constricta.

Key words: Sinonovacula constricta, ATP synthase, quantitative real-time PCR, thermal stress.