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cDNA cloning and sequencing of component C5 of proteasomes from rat hepatoma cells
Author(s) -
Tamura Tomohiro,
Tanaka Keiji,
Kumatori Atsushi,
Yamada Fumi,
Tsurumi Chizuko,
Fujiwara Tsutomu,
Ichihara Akira,
Tokunaga Fuminori,
Aruga Rie,
Iwanaga Sadaaki
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80773-c
Subject(s) - complementary dna , protein subunit , open reading frame , proteasome , protein primary structure , cdna library , peptide sequence , amino acid , homology (biology) , biochemistry , microbiology and biotechnology , biology , chemistry , gene
Proteasomes are multicatalytic proteinase complexes consisting of a set of non‐identical polypeptide subunits. A cDNA for component C5 of rat proteasomes was isolated by screening a Reuber H4TG hepatoma cell cDNA library using synthetic oligodeoxynucleotide probes corresponding to partial amino acid sequences of the protein. The polypeptide deduced from the open reading frame consisted of 240 amino acid residues with a calculated molecular weight of 26479. Computer analysis revealed little similarity of C5 to other proteins reported so far. The primary structure of C5 showed partial sequence homology to that of another component C3, but no regions of homology with the sequence of component C2. Thus C5 is concluded to be a new type of subunit of the proteasome complex.