Pulvomycin, an inhibitor of protein biosynthesis preventing ternary complex formation between elongation factor Tu, GTP, and aminoacyl-tRNA.
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Summary
Pulvomycin and the synonymous antibiotics labilomycinand 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, and the formation of the EF- Tu.GTP complex is stimulated.
- Type
- article
- Published
- 1978-11-01
- Cited by
- 44
- References
- 0
- Access
- Open access
- OpenAlex
- https://openalex.org/W1972801563
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:35384736
Keywords
GTP', Aminoacyl-tRNA, EF-Tu, Ternary complex, Ribosome
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Cited by
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- The Trp repressor, a ligand-activated regulatory protein.
- The elongation phase of protein synthesis.
- INTERACTION OF EUBACTERIAL LIGANDS WITH ARCHAEAL ELONGATION FACTOR 1α: MODULATION OF ITS MOLECULAR AND FUNCTIONAL PROPERTIES.
- Untersuchungen zur Identifizierung und Charakterisierung der EF-Tu Kinase
- Unique antibiotic sensitivity of archaebacterial polypeptide elongation factors
- Antimicrobial activities of chemically modified thiazolyl peptide antibiotic MDL 62,879 (GE2270A).
- EF-Tu, a GTPase odyssey.
- Elongation Factor Tu3 (EF-Tu3) from the Kirromycin Producer Streptomyces ramocissimus Is Resistant to Three Classes of EF-Tu-Specific Inhibitors
- Kirromycin‐resistant elongation factor Tu from wild‐type of Lactobacillus brevis
- Throwing a spanner in the works: antibiotics and the translation apparatus
- Substitution of Arg230 and Arg233 in Escherichia coli elongation factor Tu strongly enhances its pulvomycin resistance.
- The eubacterial protein synthesis inhibitor pulvomycin interacts with archaeal elongation factor 1α from Sulfolobus solfataricus.
- Targeted screening for elongation factor Tu binding antibiotics.
- Kirromycin and pulvomycin bind to different sites on the elongation-factor Tu from E. coli
- On heterogeneity of elongation factor Tu among eubacteria
- Identification of the part of kirromycin structure that acts on elongation factor Tu
- GE2270A-resistant mutations in elongation factor Tu allow productive aminoacyl-tRNA binding to EF-Tu.GTP.GE2270A complexes.
- Elongation factor Tu‐targeted antibiotics: Four different structures, two mechanisms of action
- Archaebacterial elongation factor Tu insensitive to pulvomycin and kirromycin
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