Identification of the goldfish 20S proteasome β6 subunit bound to nuclear matrix

Mika Tokumoto, Akihiko Yamaguchi, Yoshitaka Nagahama, Toshinobu Tokumoto

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Proteasomes are large, multisubunit particles that act as the proteolytic machinery for most of the regulated intracellular protein breakdown in eukaryotic cells. Proteasomes are present in both the nucleus and cytoplasm. When we analyzed the molecular composition of protein constituents of the nuclear matrix preparation of goldfish oocytes by two-dimensional polyacrylamide gel electrophoresis followed by sequence analysis, we found a 26 kDa spot identical in amino acid sequence to the β6 subunits of the 20S proteasome. No spot of other subunits of 20S proteasome was detected. Here we describe the cloning, sequencing and expression analysis of Carassius auratus, β6.

Original languageEnglish
Pages (from-to)62-66
Number of pages5
JournalFEBS Letters
Volume472
Issue number1
DOIs
Publication statusPublished - Apr 21 2000
Externally publishedYes

Fingerprint

Nuclear Matrix
Goldfish
Proteasome Endopeptidase Complex
Nuclear Matrix-Associated Proteins
Cloning
Electrophoresis, Gel, Two-Dimensional
Eukaryotic Cells
Electrophoresis
Oocytes
Machinery
Sequence Analysis
Organism Cloning
Amino Acid Sequence
Cytoplasm
Proteins
Amino Acids
Chemical analysis

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Identification of the goldfish 20S proteasome β6 subunit bound to nuclear matrix. / Tokumoto, Mika; Yamaguchi, Akihiko; Nagahama, Yoshitaka; Tokumoto, Toshinobu.

In: FEBS Letters, Vol. 472, No. 1, 21.04.2000, p. 62-66.

Research output: Contribution to journalArticle

Tokumoto, Mika ; Yamaguchi, Akihiko ; Nagahama, Yoshitaka ; Tokumoto, Toshinobu. / Identification of the goldfish 20S proteasome β6 subunit bound to nuclear matrix. In: FEBS Letters. 2000 ; Vol. 472, No. 1. pp. 62-66.
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