scholarly journals The effect of chlortetracycline on the transfer of leucine and ‘transfer’ ribonucleic acid to rat-liver ribosomes in vitro

1964 ◽  
Vol 90 (3) ◽  
pp. 624-628 ◽  
Author(s):  
TJ Franklin
Keyword(s):  
Rat Liver ◽  
Ribonucleic Acid ◽  
Liver Ribosomes

5S Ribonucleic acid-protein complex extracted from rat liver ribosomes by formamide

Biochemistry ◽  
1972 ◽  
Vol 11 (12) ◽  
pp. 2323-2326 ◽  
Author(s):  
Mary L. Petermann ◽  
Mary G. Hamilton ◽  
Amalia Pavlovec
Keyword(s):  
Rat Liver ◽  
Protein Complex ◽  
Ribonucleic Acid ◽  
Acid Protein ◽  
Liver Ribosomes

scholarly journals Inhibition of protein synthesis in vitro by crotins and ricin. Effect on the steps of peptide chain elongation

1976 ◽  
Vol 156 (1) ◽  
pp. 7-13 ◽  
Author(s):  
S Sperti ◽  
L Montanaro ◽  
A Mattioli ◽  
G Testoni ◽  
F Stirpe
Keyword(s):  
Protein Synthesis ◽  
Rat Liver ◽  
Elongation Factor ◽  
Artemia Salina ◽  
Chain Elongation ◽  
Gtp Hydrolysis ◽  
Elongation Factor 2 ◽  
The Individual ◽  
Liver Ribosomes

The effects of crotin I and crotin II on the partial reactions of polypeptide chain elongation were investigated and compared with the known effects of ricin. Crotin II was a more powerful inhibitor than crotin I, but no qualitative differences between the two crotins were found. Rat liver ribosomes, preincubated with crotins and washed through sucrose gradients, remained inactive in protein synthesis. Among the individual steps of elongation, the peptidyltransferase reaction was unaffected by crotins, but some of the reactions that involve the interaction of elongation factors 1 and 2 with ribosomes were modified. A strong inhibition of the binding of elongation factor 2 to ribosomes and a stimulation of the elongation factor2-dependent GTP hydrolysis were observed; this indicates the formation of a very unstable elongation factor 2-GDP-ribosome complex, which, however, allows a single round of translocation to take place in the presence ofelongation factor 2 and added GTP. The elongation factor 1-dependent GTP hydrolysis was inhibited by crotins, whereas the enzymic binding of aminoacyl-tRNA, to both rat liver and Artemia salina ribosomes, was scarcely affected. In a protein-synthesizing system the inhibition by crotins and by ricin leads to a block of the nascent peptides on the ribosomal aminoacyl-tRNA site, an effect consistent with inhibition at the level of translocation. The mechanism of action of crotins appears to be very similar to that of ricin.

scholarly journals Inhibition by α-amanitin of ribonucleic acid polymerase solubilized from rat liver nuclei

1970 ◽  
Vol 116 (2) ◽  
pp. 177-180 ◽  
Author(s):  
F. Novello ◽  
L. Fiume ◽  
F. Stirpe
Keyword(s):  
Rna Polymerase ◽  
Ammonium Sulphate ◽  
Rat Liver ◽  
Ribonucleic Acid ◽  
Isolated Rat Liver ◽  
Rat Liver Nuclei ◽  
Liver Nuclei ◽  
Isolated Rat

1. α-Amanitin inhibits in vitro the RNA polymerase solubilized from isolated rat liver nuclei. 2. In contrast with previous observations with whole nuclei, the inhibition occurs approximately to the same extent in the presence and in the absence of ammonium sulphate. 3. Evidence is presented that the toxin acts by interacting with the enzyme itself and not with DNA or other components.

scholarly journals Inhibition by ricin of protein synthesis in vitro: 60S ribosomal subunit as the target of the toxin (Short Communication)

1973 ◽  
Vol 136 (3) ◽  
pp. 813-815 ◽  
Author(s):  
Simonetta Sperti ◽  
Lucio Montanaro ◽  
Alessandro Mattioli ◽  
Fiorenzo Stirpe
Keyword(s):  
Protein Synthesis ◽  
Rat Liver ◽  
Short Communication ◽  
Ribosomal Subunit ◽  
Site Of Action ◽  
Liver Ribosomes

Poly(U)-directed polyphenylalanine synthesis by rat liver ribosomes is strongly inhibited by ricin. Experiments involving hybridization between subunits derived from normal and ricin-treated ribosomes demonstrate that the 60S subunit is the site of action of the toxin. The toxin inactivates the 60S subunit independently of the presence of the 40S subunit.

Phenylalanyl transfer ribonucleic acid synthetase activity associated with rat liver ribosomes and microsomes

Biochemistry ◽  
1973 ◽  
Vol 12 (20) ◽  
pp. 3859-3865 ◽  
Author(s):  
Joan S. Tscherne ◽  
Bernard Weinstein ◽  
Karl W. Lanks ◽  
Naola B. Gersten ◽  
Charles R. Cantor
Keyword(s):  
Rat Liver ◽  
Ribonucleic Acid ◽  
Synthetase Activity ◽  
Liver Ribosomes

scholarly journals Intermediate reactions in the binding of aminoacyl-transfer ribonucleic acid to rat liver ribosomes. Formation and properties of an aminoacyl-transfer ribonucleic acid–transferase I complex

1972 ◽  
Vol 126 (4) ◽  
pp. 923-931 ◽  
Author(s):  
J. Hradec
Keyword(s):  
Ion Exchange ◽  
Rat Liver ◽  
Ribonucleic Acid ◽  
Cellulose Nitrate ◽  
Stable Complex ◽  
Primary Reaction ◽  
Preparative Isolation ◽  
Reaction Proceeds ◽  
Aminoacyl Transfer ◽  
Liver Ribosomes

1. Transferase I of rat liver binds aminoacyl-tRNA to form a relatively stable complex, which is retained on cellulose nitrate filters. This reaction proceeds at both 0°C and 37°C and is inhibited by GTP. The resulting product is stabilized by GTP and Mg2+. 2. Only very low quantities of deacylated tRNA are bound by transferase I. 3. Methods are described for the preparative isolation of the transferase I–aminoacyl-tRNA complex from incubation mixtures by using ion-exchange procedures. 4. The transferase I–aminoacyl-tRNA complex becomes readily bound to ribosomes. The presence of Mg2+ is essential for the binding. GTP stimulates this reaction but is not absolutely required. 5. It is concluded that the formation of the transferase I–aminoacyl-tRNA complex may be the primary reaction in the binding of aminoacyl-tRNA to mammalian ribosomes and that, unlike in bacterial systems, GTP is not absolutely required for this step.

scholarly journals Synthesis of cyclohexylpuromycin and its reaction with N-acetylphenylalanyl-transfer ribonucleic acid on rat liver ribosomes

1975 ◽  
Vol 145 (2) ◽  
pp. 169-176 ◽  
Author(s):  
M Ariatti ◽  
A O Hawtrey
Keyword(s):  
Benzene Ring ◽  
Aromatic Ring ◽  
Rat Liver ◽  
Ribonucleic Acid ◽  
Ring System ◽  
Cyclohexane Ring ◽  
Liver Ribosomes

1. Cyclohexylpuromycin, an anlogue of puromycin in which a cyclohexane ring replaces the aromatic benzene ring of the L-phenylalanyl moeity of the nucleoside., has been synthesized and examined for its ability to release N-acetylphenylalanine from tRNA attached to rat liver ribosomes. 2.dl-Cyclohexylpuromycin was active in reacting with N-[3H]acetylphenylalanyl-tRNA on rat liver ribosomes to form N-E13H]lacetylphenylalanycyclohexypuromycin. 3. The reaction product N-acetylphenylalanylcyclohexylpuromycin and the corresponding analogue N-acetylphenylalanylpuromycin were chemically synthesized for evaluation of the structure of the released N-acetylphenylalanyl-containing material. 4. The results obtained suggest that the model of Raacke (1971) for purmycin reactivity needs further examination with regard to the role played by the aromatic ring system of the Lphenylalanyl moiety of the nucleoside

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