TilS from Escherichia coli - protein summary.
tRNA lysidine(34) synthetase
Position of modification - modification:
t:34 - k2C
Utilizes ATP and Lys as substrates. Homologs of this E.coli enzyme are present in almost all bacteria as well as in some eykaryota. In this last case, the enzyme catalyses k2C formation in mitochondrial tRNAIle(CAU). In Archaea, TilS does not exists but instead, there is a TiaS catalyzing the formation of agmatidine (C+ or agmt) in the same tRNAile(CAU) for the same decoding function as TilS in Bacteria (functional convergent type of evolution). While bacterial TilS is considered as an essential gene, it can be deleted after compensatory mutation occur in tRNAile(G34>U34AU).
An RNA-modifying enzyme that governs both the codon and amino acid specificities of isoleucine tRNA.
Soma A, Ikeuchi Y, Kanemasa S, Kobayashi K, Ogasawara N, Ote T, Kato J, Watanabe K, Sekine Y, Suzuki T
Structural basis for lysidine formation by ATP pyrophosphatase accompanied by a lysine-specific loop and a tRNA-recognition domain.
Nakanishi K, Fukai S, Ikeuchi Y, Soma A, Sekine Y, Suzuki T, Nureki O
Proc Natl Acad Sci U S A
Structural basis for translational fidelity ensured by transfer RNA lysidine synthetase.
Nakanishi K, Bonnefond L, Kimura S, Suzuki T, Ishitani R, Nureki O
Discovery and characterization of tRNAIle lysidine synthetase (TilS).
Suzuki T, Miyauchi K
Life without the essential bacterial tRNA Ile2-lysidine synthetase TilS: a case of tRNA gene recruitment in Bacillus subtilis.
Fabret C, Dervyn E, Dalmais B, Guillot A, Marck C, Grosjean H, Noirot P
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