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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Gruic-Sovulj I,Rokov-Plavec J,Weygand-Durasevic Idoi
10.1016/j.febslet.2007.09.058subject
Has Abstractpub_date
2007-10-30 00:00:00pages
5110-4issue
26eissn
0014-5793issn
1873-3468pii
S0014-5793(07)01042-3journal_volume
581pub_type
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