Characterization of CCTα and evaluating its expression in the mud crab Scylla paramamosain when chal

• 作 者: Kun Yu Jie Gong Chencui Huang Haihui Ye Guizhong Wang Chaoshu Zeng
• 机 构: CollegeofOceanandEarthSciences,XiamenUniversity,Xiamen361005,ChinaCollegeofMarineandEnvironmentalSci
• 出 处: 中国甲壳动物学会第十三次学术研讨会
• 发表日期: 2015年10期
• 关键词: Scylla paramamosain CCTα Cold hardiness Low temperature Salinity

　　Chaperonin containing the T-complex polypeptide-1 (CCT), which is known to be involved in intracellular assembly and folding of proteins, is a class of chaperonin omnipresent in all forms of life.Previous studies showed that CCT played a vital role in cold hardiness of various animals.In order to understand the response of the polypeptide complex to low temperature challenge and other environmental stresses, a subunit of CCT (CCTα) was cloned from the mud crab Scylla paramamosain by expressed sequence tag (EST) analysis and rapid amplification of cDNA ends (RACE).The full-length cDNA SpCCTα was of 1972 bp and contained a 1668 bp open reading frame (ORF) encoding a polypeptide of 555 amino acids with four conserved motifs.