cDNA cloning and sequencing of component C9 of proteasomes from rat hepatoma cells.
The nucleotide sequence of component C9 of rat proteasomes (multicatalytic proteinase complexes) has been determined from a recombinant cDNA clone isolated by screening a Reuber H4TG hepatoma cell cDNA library using synthetic oligodeoxynucleotide probes corresponding to partial amino acid sequences of the protein. The predicted sequence of C9 consists of 261 amino acid residues with a calculated molecular weight of 29,496. The C9 component is a novel protein, differing from known proteins, but its primary structure resembles those of other proteasome components, including C2, C3 and C5, although its similarity to C5 is relatively low, suggesting that proteasomes consist of a family of proteins that have evolved from a common ancestor.
Kumatori
A
A
Institute for Enzyme Research, University of Tokushima, Japan.
Tanaka
K
K
Tamura
T
T
Fujiwara
T
T
Ichihara
A
A
Tokunaga
F
F
Onikura
A
A
Iwanaga
S
S
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D003001:Cloning, Molecular; D003546:Cysteine Endopeptidases / Q000235:genetics*; D004247:DNA / Q000235:genetics / Q000302:isolation & purification; D015870:Gene Expression; D008114:Liver Neoplasms, Experimental / Q000201:enzymology*; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000235:genetics*; D046988:Proteasome Endopeptidase Complex; D051381:Rats; D015183:Restriction Mapping
D009097:Multienzyme Complexes; D004247:DNA; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex