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Related Experiment Videos

Glycinamide ribonucleotide transformylase undergoes pH-dependent dimerization

C A Mullen1, P A Jennings

  • 1Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla 92093-0359, USA.

Journal of Molecular Biology
|October 11, 1996
PubMed
Summary
This summary is machine-generated.

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Glycinamide ribonucleotide transformylase (GART) shifts from dimer to monomer as pH increases, driven by protonation changes. This pH-dependent dimerization influences enzyme activity, suggesting cellular pH can modulate GART function.

Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Glycinamide ribonucleotide transformylase (GART) crystal structures show dimers, but solution studies indicate monomeric states at optimal pH.
  • The association state of GART in solution is known to differ from its crystal structure, suggesting pH-dependent regulation.

Purpose of the Study:

  • To investigate the pH-dependent behavior of GART in solution.
  • To determine if side-chain ionization is responsible for the observed changes in GART's association state.
  • To elucidate the mechanism of pH-dependent dimerization and its impact on enzyme activity.

Main Methods:

  • Dynamic light scattering to monitor GART's association state across a pH range.
  • Difference UV-absorption spectroscopy to detect conformational changes.

Related Experiment Videos

  • Fluorescence spectroscopy to probe environmental changes around tryptophan residues.
  • Analysis of crystal structures to identify key residues at the dimer interface.

    • Main Results:

    • GART reversibly dissociates from a dimeric to a monomeric form between pH 6.8 and 7.5.
    • The dissociation fits a cooperative three-proton transfer mechanism with an apparent pKa of 7.16.
    • Conformational changes involving tyrosine residues and perturbations of tryptophan residues occur during dimerization.
    • Histidine residues (H54, H73) and tyrosine residues (Y67, Y78) at the dimer interface are implicated in pH-dependent dimerization.

    Conclusions:

    • GART exists as a mixture of monomer and dimer at physiological pH.
    • The monomer-dimer transition is sharply pH-dependent.
    • Enzyme activity is maximal in the monomeric state, suggesting that cellular pH fluctuations can modulate GART activity.