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

Thumbnail image of item number 1 in: 'Multisite phosphorylation of a synthetic peptide derived from the carboxyl terminus of the ribosomal protein S6'.
Thumbnail image of item number 2 in: 'Multisite phosphorylation of a synthetic peptide derived from the carboxyl terminus of the ribosomal protein S6'.
Thumbnail image of item number 3 in: 'Multisite phosphorylation of a synthetic peptide derived from the carboxyl terminus of the ribosomal protein S6'.
Thumbnail image of item number 4 in: 'Multisite phosphorylation of a synthetic peptide derived from the carboxyl terminus of the ribosomal protein S6'.
Showing 1-4 of 6 pages in this article.

PDF Version Also Available for Download.

Description

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.

Physical Description

6 p.

Creation Information

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

Context

This article is part of the collection entitled: UNT Scholarly Works and was provided by the UNT College of Science to the UNT Digital Library, a digital repository hosted by the UNT Libraries. More information about this article can be viewed below.

Who

People and organizations associated with either the creation of this article or its content.

Authors

Publisher

Provided By

UNT College of Science

The College of Science provides students with the high-demand skills and knowledge to succeed as researchers and professionals. The College includes four departments: Biology, Chemistry, Math, and Physics, and is also home to a number of interdisciplinary programs, centers, institutes, intercollegiate programs, labs, and services.

About | Browse this Partner

Contact Us

Corrections Questions

What

Descriptive information to help identify this article. Follow the links below to find similar items on the Digital Library.

Degree Information

Description

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.

Physical Description

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.

Source

  • Journal of Biological Chemistry, 266(1), American Society for Biochemistry and Molecular Biology, January 5 1991, pp. 380-385

Language

Item Type

Identifier

Unique identifying numbers for this article in the Digital Library or other systems.

Publication Information

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

Collections

This article is part of the following collection of related materials.

UNT Scholarly Works

Materials from the UNT community's research, creative, and scholarly activities and UNT's Open Access Repository. Access to some items in this collection may be restricted.

About | Browse this Collection

What responsibilities do I have when using this article?

Digital Files

When

Dates and time periods associated with this article.

Creation Date

  • January 5, 1991

Added to The UNT Digital Library

  • Dec. 17, 2021, 8:13 p.m.

Description Last Updated

  • Jan. 13, 2022, 11:03 a.m.

Usage Statistics

When was this article last used?

Yesterday: 0
Past 30 days: 0
Total Uses: 5
More Statistics

Interact With This Article

Here are some suggestions for what to do next.

Start Reading

Thumbnail image of item number 1 in: 'Multisite phosphorylation of a synthetic peptide derived from the carboxyl terminus of the ribosomal protein S6'.
Thumbnail image of item number 2 in: 'Multisite phosphorylation of a synthetic peptide derived from the carboxyl terminus of the ribosomal protein S6'.
Thumbnail image of item number 3 in: 'Multisite phosphorylation of a synthetic peptide derived from the carboxyl terminus of the ribosomal protein S6'.
Thumbnail image of item number 4 in: 'Multisite phosphorylation of a synthetic peptide derived from the carboxyl terminus of the ribosomal protein S6'.

PDF Version Also Available for Download.

Citations, Rights, Re-Use

International Image Interoperability Framework

IIF Logo

We support the IIIF Presentation API

Links for Robots

Helpful links in machine-readable formats.

Archival Resource Key (ARK)

International Image Interoperability Framework (IIIF)

Metadata Formats

Images

URLs

Stats

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 March 22, 2023), University of North Texas Libraries, UNT Digital Library, https://digital.library.unt.edu; crediting UNT College of Science.

Back to Top of Screen