Aminoacyl-tRNA synthetases from baker's yeast: Reacting site of enzymatic aminoacylation is not uniform for all tRNAs
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(75)81093-3/fullpdf
Reference11 articles.
1. In vitro incorporation of 2′-deoxyadenosine and 3′-deoxyadenosine into yeast tRNAPhe using tRNA nucleotidyl transferase, and properties of tRNAPhe-C-C-2′dA and tRNAPhe-C-C-3′dA
2. Accepting Site for Aminoacylation of tRNAPhe from Yeast
3. Enzymic acylation of oxdized-reduced transfer ribonucleic acid by Escherichia coli, yeast, and rat liver synthetases occurs almost exclusively at the 2'-hydroxyl
4. Unsettled questions in the field of protein synthesis
5. Affinity Elution as a Purification Method for Aminoacyl-tRNA Synthetases
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1. The tRNA A76 Hydroxyl Groups Control Partitioning of the tRNA-dependent Pre- and Post-transfer Editing Pathways in Class I tRNA Synthetase;Journal of Biological Chemistry;2015-05
2. Structural basis for recognition of cognate tRNA by tyrosyl-tRNA synthetase from three kingdoms;Nucleic Acids Research;2007-06-18
3. Partitioning of Aminoacyl-tRNA Synthetases in Two Classes Could Have Been Encoded in a Strand-Symmetric RNA World;DNA and Cell Biology;2006-11
4. Chemistry of aminoacylation and peptide bond formation on the 3′terminus of tRNA;Journal of Biosciences;2006-10
5. Participation of the tRNA A76 Hydroxyl Groups throughout Translation;Biochemistry;2006-04-25
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