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Journal archive > 2008 > N 6 November-December

FROM BACTERIA Enterococcus faecalis

K. S. Boyarshin, I. A. Kriklivyi, M. A. Tukalo

Institute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, Kyiv;
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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.

Key words: prolyl-tRNA synthetase, tRNA, editing, alanyl adenylate, hydrolysis.

The original article in Russian is available for download in PDF format.

© The Ukrainian Biochemical Journal