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Structural determination and characterization of a 40 kDa protein isolated from rat 40 S ribosomal subunit
Author(s) -
Tohgo Akira,
Takasawa Shin,
Munakata Hiroshi,
Yonekura Hideto,
Hayashi Norio,
Okamoto Hiroshi
Publication year - 1994
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(94)80188-6
Subject(s) - ribosomal protein , eukaryotic large ribosomal subunit , biology , complementary dna , peptide sequence , microbiology and biotechnology , protein subunit , ribosomal rna , biochemistry , protein primary structure , signal peptide , hspa2 , amino acid , eukaryotic small ribosomal subunit , gene , ribosome , 18s ribosomal rna , rna
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.