Structure and Dynamics of tRNA^Met Containing Core Substitutions.

ABSTRACT: The fidelity of protein synthesis is largely dominated by the accurate recognition of transfer RNAs (tRNAs) by their cognate aminoacyl-tRNA synthetases. Aminoacylation of each tRNA with its cognate amino acid is necessary to maintain the accuracy of genetic code input. Aminoacylated tRNA^Met functions in both initiation and elongation steps during protein synthesis. As a precursor to the investigation of a methionyl-tRNA synthetase-tRNA^Met complex, presented here are the results of molecular dynamics (MD) for single nucleotide substitutions in the D-loop of tRNA^Met (G15A, G18A, and G19A) probing structure/function relationships. The core of tRNA^Met likely mediates an effective communication between the tRNA anticodon and acceptor ends, contributin

SUBMITTER: Godwin RC 

PROVIDER: S-EPMC6166219 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature