How are amino acids precisely matched to their corresponding tRNAs, ensuring accurate protein synthesis? This review delves into the intricate world of aminoacyl-tRNA synthesis, a pivotal process where amino acids are linked to tRNAs based on the genetic code. It explores how aminoacyl-tRNA synthetases, the enzymes responsible for this crucial matching, achieve their remarkable precision. The paper explores the biochemical, structural, and evolutionary facets of aminoacyl-tRNA synthesis, highlighting recent studies prompted by whole-genome sequencing and structural data availability. The research elucidates the mechanisms by which aminoacyl-tRNAs are synthesized, including direct attachment, intrinsic proofreading, and extrinsic editing. This expanded and more detailed understanding of aminoacyl-tRNA synthesis is essential for deciphering the genetic code's interpretation during translation. The insights presented here offer a comprehensive resource for researchers seeking a deeper understanding of this fundamental biological process and its implications for protein synthesis and genetic fidelity. This knowledge can potentially be used in genetic engineering.
Published in the Annual Review of Biochemistry, this article aligns perfectly with the journal's focus on providing comprehensive overviews of major biochemical topics. By reviewing the latest research on aminoacyl-tRNA synthesis, the paper contributes to the journal's goal of presenting timely and authoritative syntheses of complex biological processes for a broad scientific audience. The extensive list of references further contextualizes this work within the broader field of biochemistry.
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