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Related Experiment Videos

Unisite and multisite catalysis in the ArsA ATPase.

Tongqing Zhou1, Jian Shen, Ye Liu

  • 1Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, Michigan 48201, USA.

The Journal of Biological Chemistry
|April 20, 2002
PubMed
Summary

The ArsA ATPase uses metalloid activators like arsenic (As(III)) and antimony (Sb(III)) to efficiently hydrolyze ATP. This metalloid-dependent ATP hydrolysis is crucial for the ars operon

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • The ars operon on plasmid R773 is responsible for extruding arsenic (As(III)) and antimony (Sb(III)).
  • The ArsA ATPase is the catalytic subunit of this extrusion pump, featuring two homologous nucleotide-binding domains, A1 and A2.

Purpose of the Study:

  • To investigate the mechanism of ATP hydrolysis by the ArsA ATPase.
  • To determine the role of metalloid binding in ArsA ATPase activity and its two nucleotide-binding sites.

Main Methods:

  • Utilized tryptophan fluorescence spectroscopy on a specific ArsA mutant (M446W) to monitor nucleotide binding and hydrolysis.
  • Assessed the effects of ATP, ADP, non-hydrolyzable ATP analogs, Mg(2+), and Sb(III) on fluorescence.
  • Examined ArsA mutants with altered nucleotide-binding sites (A1 and A2) to dissect domain function.

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Main Results:

  • Metalloid binding (Sb(III)) significantly accelerated ATP hydrolysis by ArsA.
  • Fluorescence quenching patterns indicated that the A2 site is primarily responsible for metalloid-activated ATP hydrolysis.
  • Mutational analysis revealed that functional A1 and A2 sites are both required for efficient multisite ATP hydrolysis in the presence of metalloids.

Conclusions:

  • The ArsA ATPase exhibits metalloid-dependent activation of ATP hydrolysis, primarily involving the A2 site.
  • The findings support a model of unisite catalysis (A1 only) in the absence of activators and multisite catalysis (A1 and A2) upon metalloid binding.