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Abstract
The chaperonin containing t-complex polypeptide 1 (CCT) assists in the ATP-dependent folding and assembly of newly translated actin and tubulin in the eukaryotic cytosol. CCT is composed of eight different subunits, each encoded by an independent gene. In this report, we used RT-PCR amplification and 5′- and 3′-rapid amplification of cDNA ends (RACE) to determine the complete cDNA sequence of the CCT delta subunit from Aedes triseriatus mosquitoes. The CCT5 cDNA is 1936 nucleotides in length and encodes a putative 533 amino acid protein with a calculated molecular mass of 57 179 daltons and pi of 7.15. Hydrophobic residues comprise 39.8% of the amino acid sequence and putative motifs for ATP-binding and ATPase-activity are present. The amino acid sequence displays strong sequence similarity to Dro-sophila melanogaster (92%), human (85%), puffer fish (84%) and mouse (84%) counterparts. CCT8 mRNA was detected in both biosynthetically active (embryo-nating) and dormant (diapausing) Ae. triseriatus embryos by RT-PCR analysis.