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D ‐Amino acids and D ‐Tyr‐tRNA Tyr deacylase: stereospecificity of the translation machine revisited
Author(s) -
Yang Hongbo,
Zheng Gen,
Peng Xiaozhong,
Qiang Boqin,
Yuan Jiangang
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00858-5
Subject(s) - transfer rna , stereospecificity , translation (biology) , chemistry , amino acid , biochemistry , stereochemistry , rna , messenger rna , gene , catalysis
Until 30 years ago, it had been considered that D ‐amino acids were excluded from living systems except for D ‐amino acids in the cell wall of microorganisms. However, D ‐amino acids, in the form of free amino acids, peptides and proteins, were recently detected in various living organisms from bacteria to mammals. The extensive distribution of bio‐functional D ‐amino acids challenges the current concept of protein synthesis: more attention should be paid to the stereospecificity of the translation machine. Besides aminoacyl‐tRNA synthetases, elongation factor Tu and some other mechanisms, D ‐Tyr‐tRNA Tyr deacylases provide a novel checkpoint since they specifically recycle misaminoacylated D ‐Tyr‐tRNA Tyr and some other D ‐aminoacyl‐tRNAs. Their unique structure represents a new class of tRNA‐dependent hydrolase. These unexpected findings have far‐reaching implications for our understanding of protein synthesis and its origin.