Heat shock protein 60 (HSP60) functions as a molecular chaperon and plays an important role in protein folding,maintenance of structural integrity and proper regulation of a subset of cytosolic proteins.To identify a sensitive biomarker of freshwater monitoring,the full-length cDNA of Tanichthys albonubes HSP60 (designated TaHSP60) was cloned by RT-PCR and RACE techniques.It was of 2 486 bp,including 5′UTR of 102 bp and 3′UTR of 656 bp.Its open reading frame contained 1 728 nucleotides which encoded a 575 amino acid peptide.The deduced amino acid sequence of T.albonubes HSP60 had the highest similarity with Danio rerio (96.2%).The similarity between T.albonubes and Carassius auratus,Paralichthys olivaceus,Salmo salari and Xenopus tropicalis was 93.2%,89.7%,88.3% and 83.8%,respectively.Clustal X analysis confirmed the existence of the typical mitochondrial signature sequence,ATP binding region and conserved GGM repeat motif at the C-terminal in T.albonubes HSP60.Phylogenetic analysis placed T.albonubes and the putative D.rerio HSP60 into one separate cluster.The results from real-time PCR showed that the T.albonubes HSP60 was ubiquitously expressed in different tissues such as liver,muscle,gill,fin clips,eye,ovary,intestine and brain. HSP60 expression levels in liver were the highest while extremely low in gill and fin clips.Statistical analysis indicated that the transcription of HSP60 in liver was significantly higher (P<0.05) than in any other organs.After copper exposed,mRNA expression level of TaHSP60 in liver were significantly higher than those in control group in 48 h and 96 h(P<0.05).The data would help design nucleotide probes for detecting HSP60 gene expressions as a biomarker in environmental monitoring.