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Chiral proofreading during protein biosynthesis and its evolutionary implications.

Pradeep Kumar1,2, Akshay Bhatnagar1, Rajan Sankaranarayanan1,2

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Summary
This summary is machine-generated.

Cellular proofreading enzymes like d-aminoacyl-tRNA deacylase (DTD) maintain homochirality essential for life. Coevolution of DTD and tRNA ensures accurate protein synthesis and was vital for eukaryogenesis.

Keywords:
Homochiralityaminoacyl-tRNA synthetasechiral proofreadingd-amino acidsendosymbiosismitochondriaprotein biosynthesistRNAtranslation of genetic codetranslation quality control

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Evolutionary Biology

Background:

  • Homochirality of biomacromolecules is crucial for life.
  • Cellular chiral checkpoints, including d-aminoacyl-tRNA deacylase (DTD), enforce this homochirality during protein biosynthesis.
  • DTD proofreads by removing incorrect d-amino acids from tRNAs, but can also remove achiral glycine.

Purpose of the Study:

  • To review recent work on DTD and tRNA^Gly coevolution.
  • To highlight the role of DTD-tRNA interactions in translation surveillance.
  • To discuss evolutionary optimizations enabling eukaryogenesis.

Main Methods:

  • Review of existing research on DTD and tRNA^Gly.
  • Analysis of coevolutionary patterns.
  • Examination of evolutionary optimization events.

Main Results:

  • DTD and tRNA^Gly coevolved to maintain translation fidelity in bacteria and eukaryotes.
  • Specific tRNA elements, like the discriminator base (N73), modulate DTD activity.
  • Two key optimization events resolved incompatibilities between archaeal and bacterial translation systems.

Conclusions:

  • DTD and tRNA^Gly coevolution is critical for accurate protein synthesis and translation surveillance.
  • Evolutionary adaptations in DTD and tRNA were essential for the emergence of mitochondria and eukaryotes.
  • Understanding these ancient mechanisms provides insights into fundamental biological processes.