cDNA cloning and sequencing of component C5 of proteasomes from rat hepatoma cells

FEBS Letters

Aruga, Rie³  Yamada, Fumi¹  Fujiwara, Tsutomu⁴  Tanaka, Keiji¹  Tokunaga, Fuminori²  Tamura, Tomohiro¹  Iwanaga, Sadaaki³  Kumatori, Atsushi¹  Tsurumi, Chizuko¹  Ichihara, Akira¹ 

[1] Institute for Enzyme Research, The University of Tokushima, Tokushima 770, Japan;Department of Molecular Biology, Graduate School of Medical Science Fukuoka 812, Japan;Department of Biology, Faculty of Science, Kyushu University 33, Fukuoka 812, Japan;Otsuka Pharmaceutical Company Ltd., Tokushima 771-01, Japan

关键词: cDNA cloning;    Multicatalytic proteinase;    Proteasome;    Subunit C5;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;    HPLC;    high-performance liquid chromatography;    bp;    base pairs;   

DOI  :  10.1016/0014-5793(90)80773-C

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown