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The tRNA His  guanylyltransferase (Thg1) transfers a guanosine triphosphate (GTP) in the 3′–5′ direction onto the 5′-terminal of tRNA His , opposite adenosine at position 73 (A 73 ). The guanosine at the −1 position (G −1 ) serves as an identity element for histidyl-tRNA synthetase. To investigate the mechanism of recognition for the insertion of GTP opposite A 73 , first we constructed a two-stranded tRNA His  molecule composed of a primer and a template strand through division at the D-loop. Next, we evaluated the structural requirements of the incoming GTP from the incorporation efficiencies of GTP analogs into the two-piece tRNA His . Nitrogen at position 7 and the 6-keto oxygen of the guanine base were important for G −1  addition; however, interestingly, the 2-amino group was found not to be essential from the highest incorporation efficiency of inosine triphosphate. Furthermore, substitution of the conserved A 73  in tRNA His  revealed that the G −1  addition reaction was more efficient onto the template containing the opposite A 73  than onto the template with cytidine (C 73 ) or other bases forming canonical Watson–Crick base-pairing. Some interaction might occur between incoming GTP and A 73 , which plays a role in the prevention of continuous templated 3′–5′ polymerization. This study provides important insights into the mechanism of accurate tRNA His  maturation.

Molecular mechanism of substrate recognition and specificity of tRNA<sup>His</sup> guanylyltransferase during nucleotide addition in the 3′–5′ direction

Molecular mechanism of substrate recognition and specificity of tRNAHis guanylyltransferase during nucleotide addition in the 3′–5′ direction

Molecular mechanism of substrate recognition and specificity of tRNA^His guanylyltransferase during nucleotide addition in the 3′–5′ direction