Multisite phosphorylation of a synthetic peptide derived from the carboxyl terminus of the ribosomal protein S6

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Article synthesizing and testing the synthetic peptide AKRRRLSSLRASTSKSESSQK (56-21) which corresponds to the carboxyl-terminal 21 amino acids of human ribosomal protein S6 as a substrate for S6/H4 kinase purified from human placenta. The data suggests that multiple S6 kinases may be required to phosphorylate S6 at all five sites which are modified in vivo.

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6 p.

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Brandon, Stanley D. & Masaracchia, Ruthann A. January 5, 1991.

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Article synthesizing and testing the synthetic peptide AKRRRLSSLRASTSKSESSQK (56-21) which corresponds to the carboxyl-terminal 21 amino acids of human ribosomal protein S6 as a substrate for S6/H4
kinase purified from human placenta. The data suggests that multiple S6 kinases may be required to phosphorylate S6 at all five sites which are modified in vivo.

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6 p.

Notes

This research was originally published in the Journal of Biological Chemistry. Brandon & Masaracchia. Multisite phosphorylation of a synthetic peptide derived from the carboxyl terminus of the ribosomal protein S6. J. Biol. Chem. 1991; 266:380-385. © the American Society for Biochemistry and Molecular Biology.

Abstract: The synthetic peptide AKRRRLSSLRASTSKSESSQK (S6-21) which corresponds to the carboxyl-terminal 21 amino acids of human ribosomal protein S6 was synthesized and tested as a substrate for S6/H4 kinase purified from human placenta. The specific activity of the enzyme with the synthetic peptide and 40 S ribosomes was 45 and 23 nmol/min/mg, respectively. The S6/H4 kinase activity with S6-21 was greater than the enzyme activity with any other substrate tested, including histones, protamine, and casein and several other synthetic peptides. The phosphorylation of the peptide was not inhibited by inhibitors of several other proteins kinases. S6/H4 kinase catalyzed the phosphorylation of three major sites in the synthetic peptide and the 40 S ribosomes. A fourth site in S6-21 was phosphorylated more slowly. The principal phosphorylation sites were serines in the acidic carboxyl-terminal domain of the peptide. A serine (Ser-7 or -8) in the amino-terminal domain was phosphorylated at approximately 25% the rate of the carboxyl-terminal domain serines. The data suggest that multiple S6 kinases may be required to phosphorylate S6 at all five sites which are modified in vivo.

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  • Journal of Biological Chemistry, 266(1), American Society for Biochemistry and Molecular Biology, January 5, 1991, pp. 1-6

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  • Publication Title: Journal of Biological Chemistry
  • Volume: 266
  • Issue: 1
  • Page Start: 380
  • Page End: 385
  • Pages: 6
  • Peer Reviewed: Yes

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  • January 5, 1991

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  • Dec. 17, 2021, 8:13 p.m.

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  • Dec. 5, 2023, 1:33 p.m.

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Brandon, Stanley D. & Masaracchia, Ruthann A. Multisite phosphorylation of a synthetic peptide derived from the carboxyl terminus of the ribosomal protein S6, article, January 5, 1991; [Rockville, Maryland]. (https://digital.library.unt.edu/ark:/67531/metadc1871044/: accessed June 24, 2024), University of North Texas Libraries, UNT Digital Library, https://digital.library.unt.edu; crediting UNT College of Science.

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