Polyuridylic Acid Stimulation of Phenylalanine in Human Ribonucleoprotein Particles

Nature ◽  
1965 ◽  
Vol 207 (4992) ◽  
pp. 95-96
Author(s):  
S. SIMBONIS
Keyword(s):  
Ribonucleoprotein Particles ◽  
Polyuridylic Acid ◽  
Stimulation Of

scholarly journals The effect of age on protein synthesis in mouse liver

1969 ◽  
Vol 113 (5) ◽  
pp. 869-878 ◽  
Author(s):  
W. I. P. Mainwaring
Keyword(s):  
Messenger Rna ◽  
Mouse Liver ◽  
Direct Evidence ◽  
Similar System ◽  
Ribonucleoprotein Particles ◽  
Polyuridylic Acid ◽  
A Cell ◽  
Rate Of Hydrolysis ◽  
Old Mice ◽  
Effect Of Age

1. A system of microsomes and 105000g supernatant from livers of old mice is less able to promote the incorporation of [14C]phenylalanine into protein than a similar system from livers of young animals. 2. The decrease in [14C]phenylalanine incorporation is attributable to changes in microsomes from old animals rather than in the cell-sap fraction. 3. Decreased synthetic ability is found in various classes of microsomes from older animals, namely unfractionated, light and heavy microsomes, but not in detergent-washed ribonucleoprotein particles. 4. Deletions of certain detergent-soluble microsomal proteins accompany the decreased synthetic ability of microsomes from older animals. 5. Microsomes from old mice are less responsive to a synthetic messenger RNA, polyuridylic acid, and this is partly due to a higher rate of hydrolysis in the presence of cell sap from animals of extreme age. 6. Other more direct evidence, from the priming of a cell-free protein-synthesizing system from bacteria and the examination of ribonucleoprotein particles on sucrose density gradients, suggests that senescence is accompanied by a decrease in messenger RNA content.

scholarly journals Stimulation of Antibacterial Vaccination in Mice by Polyadenylic Acid: Polyuridylic Acid Complex

1972 ◽  
Vol 6 (5) ◽  
pp. 699-702 ◽  
Author(s):  
Gérard Renoux ◽  
Micheline Renoux ◽  
Robert Branche
Keyword(s):  
Acid Complex ◽  
Polyadenylic Acid ◽  
Polyuridylic Acid ◽  
Stimulation Of

Stimulation of Phenylalanine Incorporation in Hepatic Polyribosome Preparations by Polyuridylic Acid

Nature ◽  
1966 ◽  
Vol 209 (5029) ◽  
pp. 1204-1206 ◽  
Author(s):  
H. BLOEMENDAL ◽  
W. S. BONT ◽  
I. MEISNER
Keyword(s):  
Polyuridylic Acid ◽  
Stimulation Of

scholarly journals Stimulation of peptide elongation by thyroxine

1976 ◽  
Vol 156 (3) ◽  
pp. 713-717 ◽  
Author(s):  
W J Carter ◽  
F H Faas ◽  
J O Wynn
Keyword(s):  
Peptide Bond ◽  
Conclusive Evidence ◽  
Chain Elongation ◽  
Synthesis System ◽  
Polyuridylic Acid ◽  
A Cell ◽  
Peptide Elongation ◽  
Trna Binding ◽  
Protein Synthesis System ◽  
Stimulation Of

This study suggests that thyroxine stimulates peptide elongation in a cell-free rat liver polyribosome system. The thyroxine effect persists in the presence of sufficient aurintricarboxylic acid to prevent polyuridylic acid-stimulated peptide initiation. In addition, thyroxine stimulates elongation of pre-existing polyphenylalanine chains providing conclusive evidence that the effect does not depend on peptide initiation. Thyroxine does not stimulate release of nascent peptides from ribosomes into the supernatant phase of the reaction mixture. Therefore in this protein-synthesis system the thyroxine effect is expected to occur at one or more of the reactions of peptide chain elongation, which include aminoacyl-tRNA binding, peptide bond synthesis and translocation.

scholarly journals Further observations on the polynucleotide-induced stimulation of protein synthesis by cell-free preparations from rabbit reticulocytes

1965 ◽  
Vol 97 (2) ◽  
pp. 595-606 ◽  
Author(s):  
KG Nair ◽  
HRV Arnstein
Keyword(s):  
Protein Synthesis ◽  
Messenger Rna ◽  
Free System ◽  
Cell Free System ◽  
Polyadenylic Acid ◽  
Polyuridylic Acid ◽  
Optimum Response ◽  
Ph Range ◽  
Rabbit Reticulocytes ◽  
Stimulation Of

1. The effect of high-molecular-weight RNA from reticulocyte polyribosomes (messenger RNA) on protein synthesis by subcellular fractions derived from reticulocytes, reported by Arnstein, Cox & Hunt (1964), has now been studied in detail. Optimum response of the cell-free system requires 30-50mm-K(+) and approx. 5mm-Mg(2+) in the pH range 7.4-7.6. 2. RNA stimulates the incorporation into protein of both free amino acids and of aminoacyl residues from s-RNA. Stimulation by either RNA or polyuridylic acid is dependent on a labile factor or enzyme, which is present in the; pH5 fraction' and may be concerned with the formation of new polysomes. Quantitatively the response of the cell-free system to RNA is similar to that of polyuridylic acid, and there appears to be competition between messenger RNA and polyuridylic acid or polyadenylic acid.

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