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Related Experiment Videos

Identity elements of tRNA(Trp). Identification and evolutionary conservation

H Xue1, W Shen, R Giegé

  • 1Department of Biochemistry, University of Toronto, Ontario, Canada.

The Journal of Biological Chemistry
|May 5, 1993
PubMed
Summary

Bacillus subtilis tryptophanyl-tRNA synthetase identifies key elements on tRNA(Trp), revealing G73 and the anticodon as major determinants. This highlights evolutionary variations in aminoacyl-tRNA synthetase identity elements across organisms.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Aminoacyl-tRNA synthetases (aaRSs) are crucial enzymes that attach specific amino acids to their cognate transfer RNAs (tRNAs).
  • The identity elements on tRNA dictate which amino acid is attached, a process vital for protein synthesis.
  • Understanding these identity elements is key to deciphering the specificity and evolution of the genetic code.

Purpose of the Study:

  • To define the identity elements on Bacillus subtilis tRNA(Trp) recognized by its cognate tryptophanyl-tRNA synthetase.
  • To investigate the varying reactivities of Bacillus subtilis tryptophanyl-tRNA synthetase towards different types of tRNAs (prokaryotic, eukaryotic, halophile).
  • To compare the identity elements of Bacillus subtilis tRNA(Trp) with those of other organisms to understand evolutionary divergence.

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Main Methods:

  • Utilized the differential reactivity of Bacillus subtilis tryptophanyl-tRNA synthetase with various tRNAs to probe tRNA(Trp) identity elements.
  • Generated mutant Bacillus subtilis tRNA(Trp) through in vivo heterologous expression in Escherichia coli and in vitro transcription using T7 RNA polymerase.
  • Compared mutant tRNA(Trp) with wild-type to identify key nucleotides responsible for aminoacylation.

Main Results:

  • Identified guanine at position 73 (G73) and the anticodon as major identity elements for Bacillus subtilis tRNA(Trp).
  • Established adenine at position 1-uracil at position 72 (A1-U72), guanine at position 5-cytosine at position 68 (G5-C68), and adenine at position 9 (A9) as minor identity elements.
  • Demonstrated that while Bacillus subtilis and Escherichia coli tryptophanyl-tRNA synthetases require G73, yeast enzymes favor a G73 to A73 replacement, indicating organism-specific variations.

Conclusions:

  • G73 and the anticodon are critical determinants for Bacillus subtilis tryptophanyl-tRNA synthetase recognition of tRNA(Trp).
  • Significant variations exist in tRNA identity elements for the same amino acid across different biological domains (prokaryotes, eukaryotes).
  • The conserved identity elements between Bacillus subtilis and Escherichia coli suggest a slower evolutionary rate for these crucial recognition sites compared to other tRNA regions.