Cloning and sequencing of the chaperonin-encoding Cctd gene from Fugu rubripes rubripes.
CCT, a chaperonin containing t-complex polypeptide 1 (TCP-1), is a cytosolic molecular chaperone involved in the folding of proteins. We have isolated the Cctd gene from a Fugu rubripes rubripes (Frr) genomic library using a rat Ccta cDNA as a probe, and cloned its cDNA by reverse transcription-polymerase chain reaction (RT-PCR) using a pair of oligodeoxyribonucleotides corresponding to the 5' and 3' non-coding regions of Frr Cctd. Cctd spans a region of 4.7 kb and consists of at least 13 exons with small introns of about 144 bp on average. The Cctd cDNA sequence revealed a deduced polypeptide of 536 amino acids sharing a high degree of homology with that of the mouse Cctd cDNA (88%). Cctd is present as a single-copy gene, as shown by genomic Southern blot analysis, and can be used for evolutionary and classification analyses of Fugu species.
Yoda
T
T
Laboratory of Food Microbiology, Osaka Prefectural Institute of Public Health, Japan.
Morita
T
T
Kawatsu
K
K
Sueki
K
K
Shibata
T
T
Hamano
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D056404:Chaperonin Containing TCP-1; D018833:Chaperonins; D018076:DNA, Complementary / Q000235:genetics; D005400:Fishes, Poisonous / Q000235:genetics*; D005796:Genes; D018832:Molecular Chaperones / Q000235:genetics*; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D018832:Molecular Chaperones; C533315:Tcp1 protein, mouse; D056404:Chaperonin Containing TCP-1; D018833:Chaperonins