Interaction of amino acyl-tRNA-synthetases from the rabbit liver with RNA and polyanions
Vol'fson, A.D.; Motorin, I.A.; Tsygankov, A.I.; Orlovskiĭ, A.F.; Gladilin, K.L.
Biokhimiia 53(5): 799-805
1988
ISSN/ISBN: 0320-9725 PMID: 3167123 Document Number: 321874
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.