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[Interaction of amino acyl-tRNA-synthetases from the rabbit liver with RNA and polyanions].

Authors: A D, Vol'fson; Iu A, Motorin; A Iu, Tsygankov; A F, Orlovskiĭ; K L, Gladilin;

[Interaction of amino acyl-tRNA-synthetases from the rabbit liver with RNA and polyanions].

Abstract

The interaction of aminoacyl-tRNA synthetase with RNA and polyanions was studied. The inhibition of the enzymes by polyU, polyI and heparin was demonstrated. It was found that this interaction is of limited specificity and is typical of single-stranded RNAs which possess no orderly secondary structure as well as of other polyanions possessing similar polyelectrolytic properties. Data from kinetic analysis and lysyl-tRNA synthetase modification by pyridoxal phosphate are suggestive of participation of the tRNA binding site in the enzyme interaction with polyanions.

Keywords

Lysine-tRNA Ligase, Poly U, Heparin, Polymers, Valine-tRNA Ligase, Arginine-tRNA Ligase, Polyelectrolytes, Amino Acyl-tRNA Synthetases, Kinetics, Liver, RNA, Transfer, Poly I, Animals, Rabbits

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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
0
Average
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