Uniform Binding of Aminoacyl-tRNAs to Elongation Factor Tu by Thermodynamic Compensation
- F. LaRiviere, A. Wolfson, O. Uhlenbeck
- Biology, ChemistryScience
- 5 October 2001
It is shown that EF-Tu binds misacylated tRNAs over a much wider range of affinities than it binds the corresponding correctly acylated t RNAs, suggesting that the protein exhibits considerable specificity for both the amino acid side chain and the tRNA body.
Modulation of tRNAAla identity by inorganic pyrophosphatase
- A. Wolfson, O. Uhlenbeck
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 30 April 2002
A highly sensitive assay of tRNA aminoacylation was developed that directly measures the fraction of aminoacylated tRNA by following amino acid attachment to the 3′-32P-labeled tRNA. When applied to…
Stable tRNA-based phylogenies using only 76 nucleotides.
- J. Widmann, J. Harris, C. Lozupone, A. Wolfson, R. Knight
- BiologyRNA: A publication of the RNA Society
- 1 August 2010
The results show that UniFrac can extract meaningful biological patterns from even phylogenies with high level of statistical inaccuracy and horizontal gene transfer, and that, overall, the pattern of tRNA evolution tracks universal phylogeny and provides a background against which to test hypotheses about the evolution of individual isoacceptors.
Diadenosine oligophosphates (Ap n A), a novel class of signalling molecules?
- L. Kisselev, J. Justesen, A. Wolfson, L. Frolova
- BiologyFEBS Letters
- 8 May 1998
Aminoacyl-tRNA synthetases from higher eukaryotes.
- L. Kisselev, A. Wolfson
- BiologyProgress in Nucleic Acid Research and Molecular…
A new assay for tRNA aminoacylation kinetics.
- A. Wolfson, J. Pleiss, O. Uhlenbeck
- Biology, ChemistryRNA: A publication of the RNA Society
- 1 August 1998
An improved quantitative assay for tRNA aminoacylation is presented based on charging of a nicked tRNA followed by separation of an aminoacylated 3'-fragment on an acidic denaturing polyacrylamide…
Mammalian valyl‐tRNA synthetase forms a complex with the first elongation factor
- Y. Motorin, A. Wolfson, A. F. Orlovsky, K. Gladilin
- Chemistry, BiologyFEBS Letters
- 10 October 1988
Purification and properties of a high-molecular-mass complex between Val-tRNA synthetase and the heavy form of elongation factor 1 from mammalian cells.
- Y. Motorin, A. Wolfson, D. Löhr, A. F. Orlovsky, K. Gladilin
- Biology, ChemistryEuropean Journal of Biochemistry
- 1 October 1991
The results strongly suggest that the complex of Val-tRNA synthetase withEF-1H is a novel functionally active individual form of EF-1, which is 10 times more active in the poly(U)-directed binding of Phe-tRNAPhe to ribosomes than EF- 1H.
Compartmentalization of certain components of the protein synthesis apparatus in mammalian cells.
- V. Popenko, J. L. Ivanova, L. Kisselev
- Biology, ChemistryEuropean Journal of Cell Biology
- 1 October 1994
The results argue in favor of compartmentalization of both free ARS (such as TrpRS) and the multi-ARS complex in the vicinity of ribosomes and implies that these enzymes may exhibit some non-canonical functions in addition to their role in protein synthesis.