Aminoacyl-tRNA synthetase activities specific to twenty amino acids in rat, rabbit and human myocardium

1973 ◽  
Vol 5 (5) ◽  
pp. 419-425 ◽  
Author(s):  
K Gibson
Keyword(s):  
Amino Acids ◽  
Trna Synthetase ◽  
Human Myocardium ◽  
Aminoacyl Trna Synthetase

scholarly journals Discovery of aminoacyl-tRNA synthetase activity through cell-surface display of noncanonical amino acids

2006 ◽  
Vol 103 (27) ◽  
pp. 10180-10185 ◽  
Author(s):  
A. J. Link ◽  
M. K. S. Vink ◽  
N. J. Agard ◽  
J. A. Prescher ◽  
C. R. Bertozzi ◽  
...  
Keyword(s):  
Amino Acids ◽  
Cell Surface ◽  
Surface Display ◽  
Cell Surface Display ◽  
Trna Synthetase ◽  
Synthetase Activity ◽  
Aminoacyl Trna Synthetase ◽  
Noncanonical Amino Acids

scholarly journals A Rationally Designed Aminoacyl-tRNA Synthetase for Genetically Encoded Fluorescent Amino Acids

2016 ◽  
Author(s):  
Ximena Steinberg ◽  
Jason Galpin ◽  
Gibran Nasir ◽  
Jose Sepulveda-Ugarte ◽  
Romina V. Sepúlveda ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Structure ◽  
Structure Function ◽  
Trna Synthetase ◽  
Aminoacyl Trna Synthetase ◽  
E Coli ◽  
Promising Strategy ◽  
Fluorescent Amino Acids

AbstractThe incorporation of non-canonical amino acids into proteins has emerged as a promising strategy to manipulate and study protein structure-function relationships with superior precision in vitro and in vivo. To date, fluorescent non-canonical amino acids (f-ncAA) have been successfully incorporated in proteins expressed in bacterial systems, Xenopus oocytes, and HEK-293T cells. Here, we describe the rational generation of an orthogonal aminoacyltRNA synthetase based on the E. coli tyrosine synthetase that is capable of encoding the f-ncAA tyr-coumarin in HEK-293T cells.

scholarly journals Studies on chemical modification of thionucleosides in the transfer ribonucleic acid of Escherichia coli

1974 ◽  
Vol 143 (2) ◽  
pp. 285-294 ◽  
Author(s):  
Yarlagadda S. Prasada Rao ◽  
Joseph D. Cherayil
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Chemical Modification ◽  
Gel Filtration ◽  
Trna Synthetase ◽  
Aminoacyl Trna Synthetase ◽  
E Coli ◽  
Chemical Reagents ◽  
Mild Conditions ◽  
Trna Species

35S-labelled tRNA from Escherichia coli was treated with chemical reagents such as CNBr, H2O2, NH2OH, I2, HNO2, KMnO4 and NaIO4, under mild conditions where the four major bases were not affected. Gel filtration of the treated tRNA showed desulphurization to various extents, depending on the nature of the reagent. The treated samples after conversion into nucleosides were chromatographed on a phosphocellulose column. NH2OH, I2 and NaIO4 reacted with all the four thionucleosides of E. coli tRNA, 4-thiouridine (s4U), 5-methylaminomethyl-2-thiouridine (mnm5s2U), 2-thiocytidine (s2C) and 2-methylthio-N6-isopentenyladenosine (ms2i6A), to various extents. CNBr, HNO2 and NaHSO3 reacted with s4U, mnm5s2U and s2C, but not with ms2i6A. KMnO4 and H2O2 were also found to react extensively with thionucleosides in tRNA. Iodine oxidation of 35S-labelled tRNA showed that only 6% of the sulphur was involved in disulphide formation. Desulphurization of E. coli tRNA with CNBr resulted in marked loss of acceptor activities for glutamic acid, glutamine and lysine. Acceptor activities for alanine, arginine, glycine, isoleucine, methionine, phenylalanine, serine, tyrosine and valine were also affected, but to a lesser extent. Five other amino acids tested were almost unaffected. These results indicate the fate of thionucleosides in tRNA when subjected to various chemical reactions and the involvement of sulphur in aminoacyl-tRNA synthetase recognition of some tRNA species of E. coli.

scholarly journals Extensive charging of transfer ribonucleic acid by bean leaf extracts in vitro

1971 ◽  
Vol 125 (4) ◽  
pp. 975-981 ◽  
Author(s):  
K. L. Tao ◽  
T. C. Hall
Keyword(s):  
Amino Acids ◽  
Calcium Phosphate ◽  
Ribonucleic Acid ◽  
Trna Synthetase ◽  
Aqueous Extracts ◽  
Aminoacyl Trna Synthetase ◽  
Leaf Extracts ◽  
Theoretical Maximum

1. Phenol was effectively removed from aqueous extracts of RNA by chromatography on Sephadex G-50. 2. Elution of tRNA from Sephadex G-50 columns at pH7.6 was shown to remove 91% of the endogenously bound amino acids. 3. tRNA prepared without recourse to ethanolic precipitation was capable of accepting much greater amounts of amino acids than could redissolved samples of precipitated tRNA. 4. Aminoacyl-tRNA synthetase enzymes were partially purified with calcium phosphate gel. Elution of enzymes from the gel at pH6.5 yielded a fraction having phenylalanine- and alanine-charging activity, but no aspartate-, lysine- or proline-charging activity, whereas elution at pH7.6 gave a fraction having aspartate-, lysine- and proline-charging activity but no phenylalanine- or alanine-charging activity. 5. By using partially synthetase enzymes and tRNA eluted from DEAE-Sephadex A-50 columns, 52% of the theoretical maximum of aminoacyl-tRNA synthesis was obtained in vitro.

scholarly journals Combinatorial Fusion Rules to Describe Codon Assignment in the Standard Genetic Code

Life ◽  
2020 ◽  
Vol 11 (1) ◽  
pp. 4
Author(s):  
Alexander Nesterov-Mueller ◽  
Roman Popov ◽  
Hervé Seligmann
Keyword(s):  
Amino Acids ◽  
Genetic Code ◽  
State Of The Art ◽  
Trna Synthetase ◽  
Aminoacyl Trna Synthetase ◽  
Standard Genetic Code ◽  
Fusion Rules ◽  
Hydrophobic Amino Acids ◽  
Combinatorial Fusion ◽  
Small Hydrophobic

We propose combinatorial fusion rules that describe the codon assignment in the standard genetic code simply and uniformly for all canonical amino acids. These rules become obvious if the origin of the standard genetic code is considered as a result of a fusion of four protocodes: Two dominant AU and GC protocodes and two recessive AU and GC protocodes. The biochemical meaning of the fusion rules consists of retaining the complementarity between cognate codons of the small hydrophobic amino acids and large charged or polar amino acids within the protocodes. The proto tRNAs were assembled in form of two kissing hairpins with 9-base and 10-base loops in the case of dominant protocodes and two 9-base loops in the case of recessive protocodes. The fusion rules reveal the connection between the stop codons, the non-canonical amino acids, pyrrolysine and selenocysteine, and deviations in the translation of mitochondria. Using fusion rules, we predicted the existence of additional amino acids that are essential for the development of the standard genetic code. The validity of the proposed partition of the genetic code into dominant and recessive protocodes is considered referring to state-of-the-art hypotheses. The formation of two aminoacyl-tRNA synthetase classes is compatible with four-protocode partition.

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