Primary structure of mammalian ribosomal protein S6

• Published in: Biochemistry (Easton) Vol. 27; no. 1; pp. 170 - 177
• Main Authors: Wettenhall, Richard E. H, Nick, Hans P, Lithgow, Trevor
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 01.01.1988
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Chromatography, High Pressure Liquid; Cyanogen Bromide; Fundamental and applied biological sciences. Psychology; Holoproteins; liver; Liver - analysis; Molecular Sequence Data; Other proteins; Peptide Fragments - analysis; Peptide Hydrolases; Proteins; Rats; Ribosomal Protein S6; Ribosomal Proteins - isolation & purification; Ribosomes - analysis; Vertebrata; Mammalia; Rat; Liver; Rodentia; Primary structure; Ribosomal protein
• ISSN: 0006-2960; 1520-4995
• DOI: 10.1021/bi00401a026

Ribosomal protein S6 was isolated from rat liver ribosomes by reversed-phase high-performance liquid chromatography (HPLC) and subjected to cyanogen bromide and proteolytic cleavages. The cleavage fragments were resolved by HPLC and sequenced by automated Edman degradation. The overall amino acid sequence of S6 (249 residues) was determined by alignment of the overlapping sequences of selected cyanogen bromide, chymotryptic, tryptic, and clostripain cleavage fragments. The only protein found to exhibit close homology with the S6 sequence is yeast ribosomal protein S10 (61% sequence identity). Previously, characterized phosphopeptide derivatives of S6 containing phosphorylation sites for adenosine 3',5'-cyclic phosphate dependent and protease-activated protein kinases originate from the carboxy-terminal region of S6 encompassing residues 233-249.