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      Isolation and characterization of a novel perchloric acid-soluble protein inhibiting cell-free protein synthesis.

      The Journal of Biological Chemistry

      Solubility, Amino Acid Sequence, Animals, Base Sequence, Blotting, Northern, Cytosol, metabolism, Heat-Shock Proteins, biosynthesis, isolation & purification, pharmacology, Liver, Male, Mass Spectrometry, Molecular Sequence Data, Open Reading Frames, Peptide Fragments, chemistry, Perchlorates, Protein Biosynthesis, drug effects, Protein Synthesis Inhibitors, Proteins, Rabbits, immunology, Rats, Rats, Wistar, Reticulocytes, Ribonucleases, Sequence Homology, Amino Acid

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          Abstract

          We found a novel protein in the postmitochondria supernatant fraction of rat liver, which is soluble in 5% perchloric acid and strongly inhibits protein synthesis in a rabbit reticulocyte lysate system. The protein extracted from the supernatant fraction with 5% perchloric acid was purified by ammonium sulfate fractionation and CM-Sephadex chromatography. The protein was shown to consist of two identical subunits with a molecular mass of 14 kDa. By immunoscreening with the rabbit antisera against the protein, a cDNA encoding the protein was cloned and sequenced. The cDNA contained an open reading frame of 411 base pairs encoding a 136-amino acid protein with a molecular mass of 14,149 Da. The deduced amino acid sequence was completely identical with that constructed from all of the above peptides. Interestingly, the perchloric acid-soluble protein inhibited cell-free protein synthesis in the rabbit reticulocyte lysate system in a different manner from RNase A. The protein is likely to inhibit an initiation stage of cell-free protein synthesis. Among the rat tissues tested, the protein was located only in liver and kidney. These findings are the first report on a new inhibitor that may be involved in the regulation of protein synthesis in those tissues.

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          8530410

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