Molecular mechanism of substrate recognition and specificity of tRNA^His guanylyltransferase during nucleotide addition in the 3'-5' direction.

ABSTRACT: 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 (A₇₃). 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 A₇₃, 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_-

SUBMITTER: Nakamura A 

PROVIDER: S-EPMC6191723 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature