Effect of modeccin on the steps of peptide-chain elongation. 1978

L Montanaro, and S Sperti, and M Zamboni, and M Denaro, and G Testoni, and A Gasperi-Campani, and F Stirpe

Modeccin inhibits polypeptide-chain elongation catalysed by Artemia salina (brine shrimp) ribosomes by inactivating the 60 S ribosomal subunit. Among the individual steps of elongation, peptide-bond formation, catalysed by 60 S peptidyltransferase, is unaffected by the toxin, whereas the binding of EF 2 (elongation factor 2) to ribosomes is strongly inhibited. Modeccin does not affect the poly(U)-dependent non-enzymic binding of either deacylated tRNAPhe or phenylalanyl-tRNA to ribosomes. The inhibitory effect of modeccin on the EF 1 (elongation factor 1)-dependent binding of phenylalanyl-tRNA is discussed, since it is decreased by tRNAPhe, which stimulates the binding reaction. The analysis of the distribution of ribosome-bound radioactivity during protein synthesis shows that modeccin consistently inhibits the radioactivity bound as long-chain peptides, but depending on the experimental conditions, can leave unchanged or even greatly stimulates the radioactivity bound as phenylalanyl-tRNA and/or short-chain peptides. It is concluded that, during the complete elongation cycle, modeccin does not affect the binding of the first aminoacyl-tRNA to ribosomes, but inhibits some step in the subsequent repetitive activity of either EF 1 or EF 2. The results obtained indicate that the mechanism of action of modeccin is very similar to that of ricin and related plant toxins such as abrin and crotin.

UI MeSH Term Description Entries
D010441 Peptide Chain Elongation, Translational A process of GENETIC TRANSLATION, when an amino acid is transferred from its cognate TRANSFER RNA to the lengthening chain of PEPTIDES. Chain Elongation, Peptide, Translational,Protein Biosynthesis Elongation,Protein Chain Elongation, Translational,Protein Translation Elongation,Translation Elongation, Genetic,Translation Elongation, Protein,Translational Elongation, Protein,Translational Peptide Chain Elongation,Biosynthesis Elongation, Protein,Elongation, Genetic Translation,Elongation, Protein Biosynthesis,Elongation, Protein Translation,Elongation, Protein Translational,Genetic Translation Elongation,Protein Translational Elongation
D010445 Peptide Elongation Factors Protein factors uniquely required during the elongation phase of protein synthesis. Elongation Factor,Elongation Factors, Peptide,Factor, Elongation,Factors, Peptide Elongation
D010649 Phenylalanine An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE. Endorphenyl,L-Phenylalanine,Phenylalanine, L-Isomer,L-Isomer Phenylalanine,Phenylalanine, L Isomer
D011072 Poly U A group of uridine ribonucleotides in which the phosphate residues of each uridine ribonucleotide act as bridges in forming diester linkages between the ribose moieties. Polyuridylic Acids,Uracil Polynucleotides,Poly(rU),Acids, Polyuridylic,Polynucleotides, Uracil
D011691 Puromycin A cinnamamido ADENOSINE found in STREPTOMYCES alboniger. It inhibits protein synthesis by binding to RNA. It is an antineoplastic and antitrypanosomal agent and is used in research as an inhibitor of protein synthesis. CL-13900,P-638,Puromycin Dihydrochloride,Puromycin Hydrochloride,Stylomycin,CL 13900,CL13900,P 638,P638
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001156 Artemia A genus of CRUSTACEA of the order ANOSTRACA, found in briny pools and lakes and often cultured for fish food. It has 168 chromosomes and differs from most crustaceans in that its blood contains hemoglobin. Brine Shrimp,Shrimp, Brine,Artemias,Brine Shrimps,Shrimps, Brine
D012270 Ribosomes Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION. Ribosome
D012346 RNA, Transfer, Amino Acyl Intermediates in protein biosynthesis. The compounds are formed from amino acids, ATP and transfer RNA, a reaction catalyzed by aminoacyl tRNA synthetase. They are key compounds in the genetic translation process. Amino Acyl tRNA,Transfer RNA, Amino Acyl,tRNA-Amino Acyl,Amino Acyl T RNA,Acyl tRNA, Amino,Acyl, tRNA-Amino,tRNA Amino Acyl,tRNA, Amino Acyl
D014118 Toxins, Biological Specific, characterizable, poisonous chemicals, often PROTEINS, with specific biological properties, including immunogenicity, produced by microbes, higher plants (PLANTS, TOXIC), or ANIMALS. Biological Toxins

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