[Interaction of amino acyl-tRNA-synthetases from the rabbit liver with RNA and polyanions].
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.
Vol'fson
A D
AD
Motorin
Iu A
IuA
Tsygankov
A Iu
AIu
Orlovskiĭ
A F
AF
Gladilin
K L
KL
D000604:Amino Acyl-tRNA Synthetases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000818:Animals; D001126:Arginine-tRNA Ligase / Q000037:antagonists & inhibitors / Q000378:metabolism; D006493:Heparin / Q000494:pharmacology; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008250:Lysine-tRNA Ligase / Q000037:antagonists & inhibitors / Q000378:metabolism; D011069:Poly I / Q000494:pharmacology; D011072:Poly U / Q000494:pharmacology; D000071228:Polyelectrolytes; D011108:Polymers / Q000378:metabolism*; D012343:RNA, Transfer / Q000378:metabolism*; D011817:Rabbits; D014637:Valine-tRNA Ligase / Q000037:antagonists & inhibitors / Q000378:metabolism
D000604:Amino Acyl-tRNA Synthetases; D001126:Arginine-tRNA Ligase; D006493:Heparin; D008250:Lysine-tRNA Ligase; D011069:Poly I; D011072:Poly U; D000071228:Polyelectrolytes; D011108:Polymers; D012343:RNA, Transfer; D014637:Valine-tRNA Ligase
Vzaimodeĭstvie aminoatil-tRNK-sintetaz iz pecheni krolika s RNK i polianionami.