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

Authors
  • Tamura, T
  • Tanaka, K
  • Kumatori, A
  • Yamada, F
  • Tsurumi, C
  • Fujiwara, T
  • Ichihara, A
  • Tokunaga, F
  • Aruga, R
  • Iwanaga, S
Type
Published Article
Journal
FEBS Letters
Publisher
Wiley (John Wiley & Sons)
Publication Date
May 07, 1990
Volume
264
Issue
1
Pages
91–94
Identifiers
PMID: 2338147
Source
Medline
License
Unknown

Abstract

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 26,479. 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.

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