[tRNA-dependent editing of errors by prolyl-tRNA synthetase from bacteria Enterococcus faecalis].
Maintenance of amino acid specificity by aminoacyl-tRNA synthetases, particularly prolyl-tRNA synthetase, requires for not only specific recognition of homologic amino acid, but also missynthesized products hydrolysis, known as editing. The speeding-up of the enzymatic hydrolysis of missynthesized alanyl adenylate by bacteria Enterococcus faecalis prolyl-tRNA synthetase in the presence of tRNAPro, and also importance for this function of 2'- and 3'-hydroxyle groups of tRNA 3'-terminal adenosine ribose is shown in the work. Furthermore, results are shown, that support the absence of editing (INS) domain role in alanyl adenylate hydrolysis. Possible significance of tRNA-dependent alanyl adenylate hydrolysis by prolyl-tRNA synthetase for prolyl-tRNAPro synthesis specificity maintenance is discussed.
Boiarshin
K S
KS
Kriklivyĭ
I A
IA
Tukalo
M A
MA
D000255:Adenosine Triphosphate / Q000378:metabolism; D000604:Amino Acyl-tRNA Synthetases / Q000037:antagonists & inhibitors* / Q000235:genetics*; D013293:Enterococcus faecalis / Q000201:enzymology* / Q000235:genetics; D006868:Hydrolysis; D016297:Mutagenesis, Site-Directed; D017433:Protein Structure, Secondary; D017393:RNA Editing; D012343:RNA, Transfer / Q000235:genetics*; D012241:Rhodopseudomonas / Q000201:enzymology / Q000235:genetics; D046249:Transfer RNA Aminoacylation
D000255:Adenosine Triphosphate; D012343:RNA, Transfer; D000604:Amino Acyl-tRNA Synthetases; C100134:prolyl T RNA synthetase