摘要
Cyclophilin D （referred to as HsCypD） was obtained from the freshwater pearl mussel （Hyriopsis schlegelil）. The full-length cDNA was 2 671 bp, encoding a protein consisting of 367 amino acids. HsCypD was determined to be a hydrophilic intracellular protein with 10 phosphorylation sites and four tetratricopeptide repeat （TPR） domains, but no signal peptide. The core sequence region YKGCIFHRIIKDFMVQGG is highly conserved in vertebrates and invertebrates. Phylogenetic tree analysis indicated that CypD from all species had a common origin, and HsCypD had the closest phylogenetic relationship with CypD from Lottia gigantea. The constitutive mRNA expression levels of HsCypD exhibited tissue-specific patterns, with the highest level detected in the intestines, followed by the gonads, and the lowest expression found in the hemocytes.
Cyclophilin D （referred to as HsCypD） was obtained from the freshwater pearl mussel （Hyriopsis schlegelil）. The full-length cDNA was 2 671 bp, encoding a protein consisting of 367 amino acids. HsCypD was determined to be a hydrophilic intracellular protein with 10 phosphorylation sites and four tetratricopeptide repeat （TPR） domains, but no signal peptide. The core sequence region YKGCIFHRIIKDFMVQGG is highly conserved in vertebrates and invertebrates. Phylogenetic tree analysis indicated that CypD from all species had a common origin, and HsCypD had the closest phylogenetic relationship with CypD from Lottia gigantea. The constitutive mRNA expression levels of HsCypD exhibited tissue-specific patterns, with the highest level detected in the intestines, followed by the gonads, and the lowest expression found in the hemocytes.
基金
supported by the National Natural Science Foundation of China(31660337)
Special Aquatic Products Industry Technology System of Jiangxi(JXARS-10)
Scientific and Technological Program of Jiangxi Province(KJLD12001,20152ACF60013 and 150166)
Natural Science Foundation of Jiangxi Province(20122BAB204016)
