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Glutaminyl-tRNA synthetase

W Freist1, D H Gauss, M Ibba

  • 1Max-Planck-Institut für experimentelle Medizin, Göttingen, Germany.

Biological Chemistry
|February 12, 1998
PubMed
Summary
This summary is machine-generated.

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Glutaminyl-tRNA synthetase (GlnRS) is a unique enzyme absent in many organisms. Its structure and function, particularly tRNA recognition, were elucidated through crystal structures and mutant analysis in E. coli.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Glutaminyl-tRNA synthetase (GlnRS) is one of twenty aminoacyl-tRNA synthetases, notable for its absence in certain organisms like gram-positive eubacteria, archaebacteria, and organelles.
  • The Escherichia coli GlnRS is a monomer of 553 amino acids (64.4 kDa), contrasting with larger mammalian counterparts that can form multienzyme complexes.

Purpose of the Study:

  • To elucidate the structural basis of glutaminyl-tRNA synthetase function.
  • To investigate the mechanism of tRNA recognition by GlnRS.
  • To understand the evolutionary relationship between GlnRS and glutamyl-tRNA synthetase.

Main Methods:

  • X-ray crystallography was employed to solve the structures of E. coli GlnRS in complex with tRNA(Gln) and ATP.

Related Experiment Videos

  • Structures were also determined for complexes with unmodified tRNA(Gln) and mutated GlnRS enzymes.
  • Mutagenesis studies using natural and artificial mutants of tRNA(Gln) and GlnRS were performed to analyze enzyme-tRNA recognition.

    • Main Results:

    • The GlnRS molecule comprises four domains, with the catalytic site located in a Rossmann fold, characteristic of class I synthetases.
    • The reaction mechanism follows the canonical adenylate pathway.
    • GlnRS primarily recognizes conventional tRNA elements, including specific bases in the anticodon loop and acceptor stem, for cognate tRNA binding.

    Conclusions:

    • The study provides detailed structural and mechanistic insights into glutaminyl-tRNA synthetase function.
    • GlnRS shares significant similarities with glutamyl-tRNA synthetase, supporting a common evolutionary origin.
    • The findings clarify the molecular basis of GlnRS-tRNA recognition in the E. coli system.