Abstract
Abstract The presence of dissolved salt during the enzymatic aminoacylation of transfer RNA diminishes the amount of aminoacyl-tRNA formed at the completion of the reaction. Experiments indicate that, although salt inhibits aminoacyl-fstRNA synthetases, the diminution of the final level of aminoacylation is the result of salt-dependent changes in tRNA. tRNAs accepting different amino acids differ widely in their sensitivity to the same salt, and each tRNA species varies considerably in its sensitivity to different substances. The salt-induced changes in tRNA can be reversed by dilution or by removal of the salt. Several physical studies have failed to reveal any measurable alteration in tRNA structure in the presence of salt concentrations in which tRNA is partially or wholly inactive in amino acid acceptance, provided Mg++ is present in all salt solutions which are compared.
Highlights
Our experiments indicate that while there is an inhibitory effect of salt on the rate of the reaction, there is a change in tRNA so that it cannot be acylated in the presence of salt solutions
At concentrations below 0.1 M, LiCl increases the amount of leucine accepted by the tRNA
The sensitivity per mole to different salt solutions bears some relationship to ionic strength, as indicated in the figure by the comparison of acceptor activity in the presence of NaCl, Na2S04, and potas
Summary
In the presence of sufficiently high salt concentrations, tRNA is entirely unable to accept amino acids. If more enzyme is added to a completed reaction in the presence of salt, no additional aminoacyl-tRNA is formed.
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
