Mode of Action of Shigella Toxin. Effects on Ribosome Structure and Function

Abstract

This research examines the primary action of Shigella dysenteriae 1 toxin as an inhibitor of eukaryotic protein biosynthesis. Two major objectives, design to reveal Shiga toxin-induced changes in ribosome structure-function relationships, are 1) to explain, in biochemical terms, the manner by which Shiga toxin enzymatically inactivates mammalian ribosomes; and 2) to define the steps of protein biosynthesis which are specifically inhibited by the toxin as a result of ribosome modification. We show that Shiga toxin is not an in vitro inhibitor of initiation of reticulocyte protein synthesis which supports existing information that the toxin is a primary inhibitor of the peptide elongation process. Changes in ribosome structure as a result of toxin action were also investigated. It was determine that Shiga toxin does not cause hydrolysis of ribosomal RNA to yield fragments larger than 10 nucleotides. Recent studies involving RNA sequencing indicate that the 3' terminal region of 5.8S ribosomal RNA remains intact following toxin inactivation of ribosomes.

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Document Details

Document Type
Technical Report
Publication Date
Aug 15, 1983
Accession Number
ADA171457

Entities

People

  • Tom G. Obrig

Organizations

  • Albany Medical College

Tags

DTIC Thesaurus Topics

  • Acids
  • Amino Acids
  • Biomedical Research
  • Cells
  • Chemistry
  • Culture Techniques
  • Epithelial Cells
  • Gel Electrophoresis
  • Gene Expression
  • Laboratory Animals
  • Mrna
  • New York
  • Proteins
  • Ribonucleic Acids
  • Toxins
  • Trna
  • Two Dimensional

Fields of Study

  • Biology
  • Computer science

Readers

  • Microbial Pathology
  • Molecular and Cellular Biochemistry