1978Proceedings of the National Academy of SciencesOpen access

Pulvomycin, an inhibitor of protein biosynthesis preventing ternary complex formation between elongation factor Tu, GTP, and aminoacyl-tRNA.

Hans Wolf, D. Assmann, Eckhard Fischer

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Abstract

Pulvomycin and the synonymous antibiotics labilomycin and 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, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated. Hydrolysis of GTP by EF-Tu, induced by aminoacyl-tRNA, ribosomes, and mRNA or by kirromycin, is inhibited by pulvomycin. As shown by Millipore filtration, chromatographic analysis, and hydrolysis protection experiments, pulvomycin prevents interaction between aminoacyl-tRNA and EF-Tu.GTP to yield the ternary complex aminoacyl-tRNA.EF-Tu.GTP. Thus, enzymatic binding of aminoacyl-tRNA to ribosomes is blocked.

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What this paper is about

Pulvomycin and the synonymous antibiotics labilomycin and 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, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated. Hydrolysis of GTP by EF-Tu, induced by aminoacyl-tRNA, ribosomes, and mRNA or by kirromycin, is inhibited by pulvomycin. As shown by Millipore filtration, chromatographic analysis, and hydrolysis protection experiments, pulvomycin prevents interaction between aminoacyl-tRNA and EF-Tu.GTP to yield the ternary complex aminoacyl-tRNA.EF-Tu.GTP. Thus, enzymatic binding of aminoacyl-tRNA to ribosomes is blocked.

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Available abstract

Pulvomycin and the synonymous antibiotics labilomycin and 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, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated. Hydrolysis of GTP by EF-Tu, induced by aminoacyl-tRNA, ribosomes, and mRNA or by kirromycin, is inhibited by pulvomycin. As shown by Millipore filtration, chromatographic analysis, and hydrolysis protection experiments, pulvomycin prevents interaction between aminoacyl-tRNA and EF-Tu.GTP to yield the ternary complex aminoacyl-tRNA.EF-Tu.GTP. Thus, enzymatic binding of aminoacyl-tRNA to ribosomes is blocked.

Key concepts: GTP', Aminoacyl-tRNA, EF-Tu, Ternary complex, Ribosome, Elongation factor, GTPase, Protein biosynthesis

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Pulvomycin, an inhibitor of protein biosynthesis preventing ternary complex formation between elongation factor Tu, GTP, and aminoacyl-tRNA. — Research Paper | ScholarLens