scholarly journals SELF-SUFFICIENCY OF NATURAL E. COLI POLYSOMES FOR AMINO ACID INCORPORATION

1964 ◽  
Vol 52 (5) ◽  
pp. 1283-1289 ◽  
Author(s):  
I. D. Raacke ◽  
J. Fiala
Keyword(s):  
Amino Acid ◽  
Amino Acid Incorporation ◽  
E Coli ◽  
Acid Incorporation ◽  
Self Sufficiency

Amino acid incorporation into protein by extracts of E. coli

1960 ◽  
Vol 42 ◽  
pp. 206-211 ◽  
Author(s):  
Marvin R. Lamborg ◽  
Paul C. Zamecnik
Keyword(s):  
Amino Acid ◽  
Amino Acid Incorporation ◽  
E Coli ◽  
Acid Incorporation

Performance of optimized noncanonical amino acid mutagenesis systems in the absence of release factor 1

2016 ◽  
Vol 12 (6) ◽  
pp. 1746-1749 ◽  
Author(s):  
Yunan Zheng ◽  
Marc J. Lajoie ◽  
James S. Italia ◽  
Melissa A. Chin ◽  
George M. Church ◽  
...  
Keyword(s):  
Amino Acid ◽  
Release Factor ◽  
Amino Acid Incorporation ◽  
E Coli ◽  
Acid Incorporation ◽  
Amino Acid Mutagenesis ◽  
Noncanonical Amino Acid

Unconditional deletion of RF1 in a genomically recoded E. coli enables multisite noncanonical amino acid incorporation by UAG suppression.

scholarly journals Combining site-directed spin labeling in vivo and in-cell EPR distance determination

2020 ◽  
Vol 22 (9) ◽  
pp. 4875-4879 ◽  
Author(s):  
Pia Widder ◽  
Julian Schuck ◽  
Daniel Summerer ◽  
Malte Drescher
Keyword(s):  
Amino Acid ◽  
Stop Codon ◽  
Spin Labeling ◽  
Amino Acid Incorporation ◽  
Distance Determination ◽  
E Coli ◽  
Acid Incorporation ◽  
Canonical Amino Acid ◽  
Site Directed Spin Labeling

Non-canonical amino acid incorporation via amber stop codon suppression and in vivo site-directed spin labeling allow in-cell EPR distance determination in E. coli.

Further studies on eukaryote DNA stimulation of amino acid incorporation in E. coli extracts

1974 ◽  
Vol 160 (2) ◽  
pp. 603-613
Author(s):  
Nando K. Chatterjee ◽  
De-Maw Chuang ◽  
Herbert Weissbach
Keyword(s):  
Amino Acid ◽  
Amino Acid Incorporation ◽  
E Coli ◽  
Acid Incorporation ◽  
Stimulation Of

scholarly journals Studies on the inhibition of protein synthesis by selenodiglutathione

1979 ◽  
Vol 180 (1) ◽  
pp. 213-218 ◽  
Author(s):  
L N Vernie ◽  
J G Collard ◽  
A P Eker ◽  
A de Wildt ◽  
I T Wilders
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Elongation Factor ◽  
Amino Acid Incorporation ◽  
Free System ◽  
Cell Free System ◽  
E Coli ◽  
Acid Incorporation ◽  
F Cells ◽  
A Cell

Amino acid incorporation in a cell-free system derived from rat liver has previously been found to be inhibited by GSSeSG (selenodiglutathione). In the present experiments the effect of GSSeSG on protein synthesis in 3T3-f cells, on growth and protein synthesis in Escherichia coli, and on amino acid incorporation in a cell-free system derived from E. coli, was studied. GSSeSG inhibits the incorporation of [3H]leucine into protein by 3T3-f cells. This inhibition cannot be reversed by removing GSSeSG and is correlated with the uptake of GSSeSG. Sodium selenite (Na2SeO3) and oxidized glutathione had no inhibitory effect in this system. [3H]Uridine or [3H]thymidine incorporation into RNA or DNA was not inhibited, indicating that the primary action of GSSeSG was on protein synthesis. GSSeSG did not influence the growth of E. coli in a synthetic medium, although enhanced amino acid incorporation was observed. In the cell-free system derived from E. coli, amino acid incorporation was not changed by GSSeSG, indicating that elongation factor G, in contrast to elongation factor 2 of mammalian cell systems, is not blocked by GSSeSG.

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