scholarly journals Lack of inhibition by l-1-chloro-4-phenyl-3-toluene-p-sulphoamidobutan-2-one (l-1-tosylamido-2-phenylethyl chloromethyl ketone) of the formation of bacterial polypeptide chain initiation complex (Short Communication)

1973 ◽  
Vol 136 (2) ◽  
pp. 433-436 ◽  
Author(s):  
J. Jonák ◽  
B. F. C. Clark
Keyword(s):  
Short Communication ◽  
Polypeptide Chain ◽  
Protein Biosynthesis ◽  
Elongation Factor ◽  
Initiation Factor ◽  
Chain Elongation ◽  
Initiation Complex ◽  
Chloromethyl Ketone ◽  
Chain Initiation

The chymotrypsin inhibitor l-1-chloro-4-phenyl-3-toluene-p-sulphonamidobutan-2-one does not inhibit the function of the initiation factor during the formation of the polypeptide chain initiation complex in vitro. Since the inhibitor has been shown previously to inhibit polypeptide chain elongation by reacting with elongation factor EF-Tu, the inhibitor can be used to investigate the initiation and elongation steps of protein biosynthesis separately.

scholarly journals Protein synthesis in vitro in a system from plant mitochondria (Short Communication)

1973 ◽  
Vol 134 (3) ◽  
pp. 815-816 ◽  
Author(s):  
Biswendu B. Goswami ◽  
Symamalima Chakrabarti ◽  
Dipak K. Dube ◽  
S. C. Roy
Keyword(s):  
Short Communication ◽  
Potent Inhibitor ◽  
Plant Mitochondria ◽  
Elongation Factor ◽  
Chain Elongation ◽  
Vigna Sinensis ◽  
Highly Sensitive ◽  
S 100 ◽  
Germinating Seeds

A mitochondrial system from 48h-germinating seeds of Vigna sinensis (Linn.) Savi is capable of incorporating l-[U-14C]valine into proteins and is practically insensitve to cycloheximide, but highly sensitive to chloramphenicol and fusidic acid, a potent inhibitor of peptide-chain elongation factor. A system consisting of mitochondrial S-100 fraction and ribosomes from the same source and other cofactors is capable of polyphenylalanine synthesis and behaves similarly with respect to these inhibitors.

scholarly journals Inhibition by ricin of protein synthesis in vitro. Inhibition of the binding of elongation factor 2 and of adenosine diphosphate-ribosylated elongation factor 2 to ribosomes

1975 ◽  
Vol 146 (1) ◽  
pp. 127-131 ◽  
Author(s):  
L Montanaro ◽  
S Sperti ◽  
A Mattioli ◽  
G Testoni ◽  
F Stirpe
Keyword(s):  
Protein Synthesis ◽  
Binding Sites ◽  
Polypeptide Chain ◽  
Elongation Factor ◽  
Adenosine Diphosphate ◽  
Chain Elongation ◽  
Elongation Factor 2 ◽  
In Vitro Inhibition ◽  
Liver Ribosomes

The binding of EF2 (elongation factor 2) and of ADP-ribosyl-EF 2 to rat liver ribosomes is inhibited by ricin. This result suggests that the native enzyme and its ADP-ribose derivative have the same or closely related binding sites on the ribosome. The inhibition by ricin of the binding of EF 2 to ribosomes is consistent with the previous observation that ricin affects EF 2-catalysed translocation during polypeptide chain elongation.

scholarly journals Identification of Novel Inhibitors of Bacterial Translation Elongation Factors

2005 ◽  
Vol 49 (1) ◽  
pp. 131-136 ◽  
Author(s):  
Maithri M. K. Jayasekera ◽  
Keysha Onheiber ◽  
John Keith ◽  
Hariharan Venkatesan ◽  
Alejandro Santillan ◽  
...  
Keyword(s):  
Protein Biosynthesis ◽  
Elongation Factor ◽  
Chain Elongation ◽  
Metabolic Labeling ◽  
Chemical Library ◽  
Translation Elongation ◽  
Gram Positive Bacteria ◽  
Bacterial Transcription ◽  
Bacterial Translation

ABSTRACT Bacterial elongation factor Tu (EF-Tu) and EF-Ts are interacting proteins involved in polypeptide chain elongation in protein biosynthesis. A novel scintillation proximity assay for the detection of inhibitors of EF-Tu and EF-Ts, as well as the interaction between them, was developed and used in a high-throughput screen of a chemical library. Several compounds from a variety of chemical series with inhibitory properties were identified, including certain indole dipeptides, benzimidazole amidines, 2-arylbenzimidazoles, N-substituted imidazoles, and N-substituted guanidines. The in vitro activities of these compounds were confirmed in a coupled bacterial transcription-translation assay. Several indole dipeptides were identified as inhibitors of bacterial translation, with compound 2 exhibiting a 50% inhibitory concentration of 14 μM and an MIC for S. aureus ATCC 29213 of 5.6 μg/ml. Structure-activity relationship studies around the dipeptidic indoles generated additional analogs with low micromolar MICs for both gram-negative and gram-positive bacteria. To assess the specificity of antibacterial action, these compounds were evaluated in a metabolic labeling assay with Staphylococcus aureus. Inhibition of translation, as well as limited effects on other macromolecular pathways for some of the analogs studied, indicated a possible contribution from a non-target-based antibacterial mechanism of action.

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