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A mini Alanyl-tRNA synthetase (AlaRS) from Tupanvirus lacks key domains but still recognizes tRNAAla. This suggests a novel tRNA-binding mechanism evolved in this unique virus.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Virology

Background:

  • Alanyl-tRNA synthetase (AlaRS) typically has catalytic, tRNA-recognition, editing, and C-Ala domains.
  • The C-Ala domain is crucial for binding the elbow of tRNAAla.
  • A truncated AlaRS (mini-AlaRS) lacking editing and C-Ala domains was found in Tupanvirus.

Purpose of the Study:

  • To investigate the structure and function of Tupanvirus AlaRS (TuAlaRS).
  • To determine how TuAlaRS recognizes tRNAAla despite lacking conserved domains.
  • To explore the tRNA-binding mode of this mini-AlaRS.

Main Methods:

  • Phylogenetic analysis of TuAlaRS.
  • Biochemical assays to assess tRNAAla binding and aminoacylation.
  • In vivo functional complementation assays in yeast.

Main Results:

  • TuAlaRS is phylogenetically related to host AlaRS.
  • Despite lacking canonical recognition residues, TuAlaRS specifically binds G3:U70 in tRNAAla.
  • TuAlaRS binds and charges tRNAAla and microAla, indicating acceptor stem targeting.
  • Mini-AlaRS functionally substitutes for yeast AlaRS in vivo.

Conclusions:

  • TuAlaRS utilizes a novel tRNA-binding mode.
  • The loss of the C-Ala domain is compensated by an alternative mechanism.
  • This finding offers insights into the evolution of aminoacyl-tRNA synthetases in viruses.