Structural determination and characterization of a 40 kDa protein isolated from rat 40 S ribosomal subunit

Akira Tohgo, Shin Takasawa, Hiroshi Munakata, Hideto Yonekura, Norio Hayashi, Hiroshi Okamoto

Research output: Contribution to journalArticlepeer-review

38 Citations (Scopus)

Abstract

We have purified a 40 kDa protein from the rat 40 S ribosomal subunit and determined its primary structure by amino acid and cDNA sequencing. The amino acid sequence of the 40 kDa protein shared 29-37% homology with prokaryotic ribosomal protein S2 of eubacteria and chloroplasts, indicating that the protein is a eukaryotic counterpart to prokaryotic S2. Moreover, the amino acid sequence shared 99% identity with those deduced from cDNAs for 68 kDa laminin binding proteins of human, murine and bovine origins. The cDNAs are capable of encoding polypeptides with predicted molecular mass of 33,000 which lacked typical signal sequences, N-linked glycosylation sites and putative transmembrane domains. These results indicate that the eDNAs for 68 kDa laminin binding proteins actually code for the 40 kDa ribosomal protein.

Original languageEnglish
Pages (from-to)133-138
Number of pages6
JournalFEBS Letters
Volume340
Issue number1-2
DOIs
Publication statusPublished - 1994 Feb 28

Keywords

  • 68 kDa laminin binding protein
  • Amino acid sequence
  • Rat liver
  • Ribosomal protein S2
  • cDNA cloning

ASJC Scopus subject areas

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

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