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

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 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

Structural Ribonucleic Acid of Rat-Liver Ribosomes

1964 ◽  
Vol 91 (3) ◽  
pp. 21C-32C ◽  
Author(s):  
A. J. Munro
Keyword(s):  
Rat Liver ◽  
Ribonucleic Acid ◽  
Liver Ribosomes

Stimulation by Rat Liver Ribonucleic Acid of Incorporation of Amino-acid into Rat Liver Ribosomes

Nature ◽  
1963 ◽  
Vol 199 (4892) ◽  
pp. 489-490 ◽  
Author(s):  
A. KORNER ◽  
A. J. MUNRO
Keyword(s):  
Amino Acid ◽  
Rat Liver ◽  
Ribonucleic Acid ◽  
Liver Ribosomes

Degradation of ribonucleic acid in rat liver ribosomes

1973 ◽  
Vol 76 (4) ◽  
pp. 425-444 ◽  
Author(s):  
G.N. Dessev ◽  
K. Grancharov
Keyword(s):  
Rat Liver ◽  
Ribonucleic Acid ◽  
Liver Ribosomes

Interaction between rat-liver ribosomes and soluble ribonucleic acid

1963 ◽  
Vol 68 ◽  
pp. 487-490 ◽  
Author(s):  
W.S. Bont ◽  
L. Bosch ◽  
H. Bloemendal ◽  
H. Hilders ◽  
F. Huizinga
Keyword(s):  
Rat Liver ◽  
Ribonucleic Acid ◽  
Liver Ribosomes

scholarly journals Intermediate reactions in the binding of aminoacyl-transfer ribonucleic acid to rat liver ribosomes. The interaction of cholesteryl 14-methylhexadecanoate

1972 ◽  
Vol 126 (5) ◽  
pp. 1225-1229 ◽  
Author(s):  
J. Hradec
Keyword(s):  
Binding Site ◽  
Rat Liver ◽  
Ribonucleic Acid ◽  
Binding Capacity ◽  
Original Activity ◽  
Aminoacyl Transfer ◽  
Liver Ribosomes

1. Transferase I from rat liver extracted with iso-octane binds significantly less aminoacyl-tRNA than the non-extracted enzyme. The original activity can be fully restored by the addition of cholesteryl 14-methylhexadecanoate. The binding capacity for GTP is not affected by the extraction. 2. In the presence of extracted transferase I the binding of aminoacyl-tRNA to ribosomes is decreased to 11–26% and the simultaneous binding of GTP to 32–43%. Cholesteryl 14-methylhexadecanoate induces a full reactivation of the extracted enzyme in both respects. 3. Extracted complexes A (aminoacyl-tRNA–GTP–transferase I) become bound to ribosomes to the same extent as the corresponding non-extracted preparations. 4. It is concluded that cholesteryl 14-methylhexadecanoate interacts with the binding site of transferase I for aminoacyl-tRNA and secondarily with that for GTP. It does not affect the binding site for ribosomes.

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