PMID:17931630
| Citation |
Gruic-Sovulj, I, Rokov-Plavec, J and Weygand-Durasevic, I (2007) Hydrolysis of non-cognate aminoacyl-adenylates by a class II aminoacyl-tRNA synthetase lacking an editing domain. FEBS Lett. 581:5110-4 |
|---|---|
| Abstract |
Aminoacyl-tRNA synthetases, a group of enzymes catalyzing aminoacyl-tRNA formation, may possess inherent editing activity to clear mistakes arising through the selection of non-cognate amino acid. It is generally assumed that both editing substrates, non-cognate aminoacyl-adenylate and misacylated tRNA, are hydrolyzed at the same editing domain, distant from the active site. Here, we present the first example of an aminoacyl-tRNA synthetase (seryl-tRNA synthetase) that naturally lacks an editing domain, but possesses a hydrolytic activity toward non-cognate aminoacyl-adenylates. Our data reveal that tRNA-independent pre-transfer editing may proceed within the enzyme active site without shuttling the non-cognate aminoacyl-adenylate intermediate to the remote editing site. |
| Links |
PubMed Online version:10.1016/j.febslet.2007.09.058 |
| Keywords |
Adenosine Monophosphate/chemistry; Binding Sites; Cysteine/chemistry; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Hydrolysis; Protein Structure, Tertiary; RNA Editing; Saccharomyces cerevisiae Proteins/chemistry; Saccharomyces cerevisiae Proteins/genetics; Serine/analogs & derivatives; Serine/chemistry; Serine-tRNA Ligase/chemistry; Serine-tRNA Ligase/genetics; Substrate Specificity; Threonine/chemistry |
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