D-Amino acids and D-Tyr-tRNA(Tyr) deacylase: stereospecificity of the translation machine revisited

FEBS Lett. 2003 Sep 25;552(2-3):95-8. doi: 10.1016/s0014-5793(03)00858-5.

Abstract

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.

Publication types

  • Review

MeSH terms

  • Amino Acids / chemistry*
  • Amino Acids / metabolism*
  • Aminoacyltransferases / chemistry*
  • Aminoacyltransferases / metabolism*
  • Animals
  • Catalytic Domain
  • Humans
  • Models, Molecular
  • Protein Biosynthesis
  • Protein Conformation
  • RNA, Transfer, Amino Acyl / chemistry
  • RNA, Transfer, Amino Acyl / metabolism
  • Stereoisomerism
  • Substrate Specificity

Substances

  • Amino Acids
  • RNA, Transfer, Amino Acyl
  • Aminoacyltransferases
  • D-tyrosine tRNA(Tyr) deacylase