NAD dependent inhibition of protein synthesis by Pseudomonas aeruginosa toxin

B. H. Iglewski, David Kabat

Research output: Contribution to journalArticle

354 Citations (Scopus)

Abstract

P. aeruginosa toxin (PA toxin) inhibits protein synthesis in a reticulocyte cell free system. The inhibition requires NAD and results in a block at an elongation step of polypeptide assembly. PA toxin was found to act like diphtheria toxin fragment A. Both toxins catalyze the transfer of radioactivity from nicotinamide (U 14C) adenine dinucleotide ([14C]NAD) into covalent linkage with the 100,000 dalton elongation factor 2 (EF 2) protein. Furthermore, in the presence of a limiting amount of EF 2, excess toxin, and [14C] NAD, the two toxins were non additive in the amount of label transferred to EF 2. Unlike free fragment A of diphtheria toxin, the enzymatic activity of PA toxin is heat labile and neutralizable with antibody to PA toxin but not with antibody to fragment A. Although PA and diphtheria toxins have different cellular specificities and molecular properties and produce different clinical symptoms, their intracellular mechanisms of action appear to be identical.

Original languageEnglish (US)
Pages (from-to)2284-2288
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume72
Issue number6
StatePublished - 1975

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Peptide Elongation Factor 2
NAD
Pseudomonas aeruginosa
Diphtheria Toxin
Proteins
Immunoglobulin Fragments
Niacinamide
Cell-Free System
Reticulocytes
Adenine
Radioactivity
Hot Temperature
Peptides
Antibodies

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

NAD dependent inhibition of protein synthesis by Pseudomonas aeruginosa toxin. / Iglewski, B. H.; Kabat, David.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 72, No. 6, 1975, p. 2284-2288.

Research output: Contribution to journalArticle

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