Genomic organization of tRNA and aminoacyl-tRNA synthetase genes for two amino acids in Saccharomyces cerevisiae

Genomics ◽  
1988 ◽  
Vol 3 (3) ◽  
pp. 201-206 ◽  
Author(s):  
Connie J. Kolman ◽  
Michael Snyder ◽  
Dieter Söll
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Genomic Organization ◽  
Trna Synthetase ◽  
Aminoacyl Trna Synthetase

scholarly journals Aminoacyl-tRNA synthetase complex in Saccharomyces cerevisiae

1995 ◽  
Vol 309 (1) ◽  
pp. 321-324 ◽  
Author(s):  
C L Harris ◽  
C J Kolanko
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Density Gradient Centrifugation ◽  
Gradient Centrifugation ◽  
Sucrose Density Gradient ◽  
Trna Synthetase ◽  
Synthetase Activity ◽  
Aminoacyl Trna Synthetase ◽  
Sucrose Density Gradient Centrifugation ◽  
Cell Extracts ◽  
Molecular Masses

The size distribution of aminoacyl-tRNA synthetase activity was investigated in cell extracts prepared from Saccharomyces cerevisiae. Bio-Gel A-5M chromatography of 105,000 g supernatants separated isoleucyl-tRNA synthetase activity into three peaks, with apparent molecular masses (Da) of about 100,000, 350,000 and 10(6) or greater. Similar results were obtained with synthetases specific for glutamic acid, serine and tyrosine. Sucrose-density-gradient centrifugation of yeast supernatants also provided evidence for the existence of synthetase complexes. These data provide the first evidence for the existence of a high-molecular-mass aminoacyl-tRNA synthetase complex in yeast, perhaps similar to those reported in higher eukaryotes.

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.

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