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NAD-dependent inhibition of protein synthesis by Pseudomonas aeruginosa toxin,.

Open access
Iglewski, B H, Kabat, D·1975·Proceedings of the National Academy of Sciences

Abstract

Pseudomonas 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-14-C)adenine dinucleotide ((14-C)NAD) into covalent linkage with the 100,000 dalton elongation (EF-2) protein. Furthermore, in the presence of a limiting amount of EF-2, excess toxin, and (14-C)NAD, the two toxins were non-additive in the amount of label transferred to EF-3. 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.

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Metadata

Authors
Iglewski, B. H., & Kabat, D.
Venue
Proceedings of the National Academy of Sciences
Published
1975-06
Volume
72
Issue
6
Pages
2284-2288
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2014335282
Cited by
620
References
0
FWCI
7.85
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: NAD-dependent inhibition of protein synthesis by Pseudomonas aeruginosa toxin,. https://app.cochat.ai/papers/10.1073/pnas.72.6.2284
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Iglewski, B. H., & Kabat, D. (1975). NAD-dependent inhibition of protein synthesis by Pseudomonas aeruginosa toxin,. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.72.6.2284

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.