Phenylalanyl transfer ribonucleic acid synthetase from rat liver. Analysis of phenylalanine and adenosine 5'-triphosphate binding sites and comparison to the enzyme from Escherichia coli

1976 ◽  
Vol 19 (11) ◽  
pp. 1276-1279 ◽  
Author(s):  
Daniel V. Santi ◽  
Robert W. Webster
Keyword(s):  
Escherichia Coli ◽  
Rat Liver ◽  
Ribonucleic Acid ◽  
Binding Sites

Binding Sites on Escherichia coli Ribonucleic Acid Polymerase

1976 ◽  
Vol 4 (4) ◽  
pp. 633-634 ◽  
Author(s):  
A. GRAHAM ◽  
J. GREENE ◽  
P. A. LOWE ◽  
A. D. B. MALCOLM
Keyword(s):  
Escherichia Coli ◽  
Ribonucleic Acid ◽  
Binding Sites

scholarly journals Changes in the number of binding sites for ribonucleic acid polymerase in chromatin of WI-38 fibroblasts stimulated to proliferate

1974 ◽  
Vol 141 (1) ◽  
pp. 27-34 ◽  
Author(s):  
Bridget T. Hill ◽  
Renato Baserga
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Rna Polymerase ◽  
Ribonucleic Acid ◽  
Binding Sites ◽  
Template Activity ◽  
E Coli ◽  
Human Diploid Fibroblasts ◽  
Chromatin Template ◽  
Number Of Binding Sites

1. When WI-38 human diploid fibroblasts form confluent monolayers, DNA synthesis and cell division almost completely cease. A change of medium causes these density-inhibited cells to proliferate and within 1h after the application of the stimulus there is an increase in template activity of the chromatin isolated from stimulated cells. 2. The number of binding sites for Escherichia coli RNA polymerase was determined on chromatin from WI-38 cells by two different methods, i.e. incorporation of [3H]UTP into RNA in the absence of reinitiation, and incorporation of [γ-32P]GTP into chain termini. 3. Both methods indicate that the capacity of chromatin to bind E. coli RNA polymerase is increased in WI-38 cells stimulated to proliferate. 4. The increase in the number of binding sites for E. coli RNA polymerase parallels the increase in chromatin template activity and suggests that the latter reflects an increase in the number of initiation sites, rather than an increase in the rate of transcription.

Enzymic acylation of oxdized-reduced transfer ribonucleic acid by Escherichia coli, yeast, and rat liver synthetases occurs almost exclusively at the 2'-hydroxyl

Biochemistry ◽  
1974 ◽  
Vol 13 (26) ◽  
pp. 5425-5432 ◽  
Author(s):  
James Ofengand ◽  
Stanislav Chladek ◽  
George Robilard ◽  
Joan Bierbaum
Keyword(s):  
Escherichia Coli ◽  
Rat Liver ◽  
Ribonucleic Acid

scholarly journals Synthesis of thiol-containing analogues of puromycin and a study of their interaction with N-acetylphenylalanyl-transfer ribonucleic acid on ribosomes to form thioesters

1975 ◽  
Vol 149 (1) ◽  
pp. 209-220 ◽  
Author(s):  
John Gooch ◽  
Arthur O. Hawtrey
Keyword(s):  
Escherichia Coli ◽  
Rat Liver ◽  
Ribonucleic Acid ◽  
Incubation Medium ◽  
Amino Group ◽  
Marked Contrast ◽  
E Coli ◽  
Primary Amino ◽  
Compound Xvii

1. The thiol-containing analogue of puromycin, 6-dimethylamino-9-{1′-[3′-(2″-mercapto-3″-phenylpropionamido)-3′-deoxy-β-d-ribofuranosyl]}purine (XVII) in which the primary amino group of the antibiotic is replaced with a thiol grouping, was synthesized chemically (compound XVII is abbreviated to thiopuromycin). 2. Thiopuromycin (XVII) was found to be active in releasing N-[3H]acetylphenylalanine from its tRNA carrier as the thioester, N-acetylphenylalanylthiopuromycin (XIX) in the Escherichia coli ribosomal system. The reaction product (XIX) was synthesized chemically from thiopuromycin and N-acetylphenylalanine and found to be stable to hydrolysis in the standard incubation medium at pH7.6. dl-Phenyl-lactylpuromycin (XXI), the hydroxy analogue of puromycin, was also synthesized chemically and shown to release N-acetylphenylalanine from its tRNA carrier in the E. coli ribosomal system, thus confirming the previous results of Fahnestock et al. [Biochemistry (1970) 9, 2477–2483]. 3. In marked contrast with the results obtained in the E. coli system, both thiopuromycin (XVII) and hydroxypuromycin (XXI) were found to be inactive in releasing N-acetylphenylalanine from its tRNA carrier in the rat liver ribosomal system.

scholarly journals Biosynthesis of N-(purin-6-ylcarbamoyl)-l-threonine riboside. Incorporation of l-threonine in vivo into modified nucleoside of transfer ribonucleic acid

1972 ◽  
Vol 127 (3) ◽  
pp. 515-519 ◽  
Author(s):  
Girish B. Chheda ◽  
Chung Il Hong ◽  
Conrad F. Piskorz ◽  
G. A. Harmon
Keyword(s):  
Escherichia Coli ◽  
Rat Liver ◽  
Ribonucleic Acid ◽  
Modified Nucleoside

l-[U-14C]Threonine is incorporated into N-(purin-6-ylcarbamoyl)-l-threonine riboside of rat liver and Escherichia coli tRNA. A pathway is suggested for the biosynthesis of this nucleoside.

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