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.
Laboratory of Food Microbiology, Osaka Prefectural Institute of Public Health, Japan.
T
T
Yoda
T
T
Morita
K
K
Kawatsu
K
K
Sueki
T
T
Shibata
Y
Y
Hamano
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