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Hydrolysis of non‐cognate aminoacyl‐adenylates by a class II aminoacyl‐tRNA synthetase lacking an editing domain
Author(s) -
Gruic-Sovulj Ita,
Rokov-Plavec Jasmina,
Weygand-Durasevic Ivana
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.09.058
Subject(s) - aminoacyl trna synthetase , transfer rna , aminoacyl trna , amino acyl trna synthetases , adenylate kinase , amino acid , biochemistry , cognate , enzyme , biology , chemistry , rna , linguistics , philosophy , gene
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.