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Related Experiment Videos

The ATP-metallothionein complex

L J Jiang1, W Maret, B L Vallee

  • 1Center for Biochemical and Biophysical Sciences and Medicine, Harvard Medical School, Seeley G. Mudd Building, 250 Longwood Avenue, Boston, MA 02115, USA.

Proceedings of the National Academy of Sciences of the United States of America
|August 5, 1998
PubMed
Summary
This summary is machine-generated.

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Metallothionein (MT) binds ATP, enhancing zinc transfer and reactivity. This suggests MT actively distributes zinc, influenced by cellular redox and energy states.

Area of Science:

  • Biochemistry
  • Metalloprotein research
  • Cellular signaling

Background:

  • Metallothionein (MT) is known to interact with glutathione (GSH) and glutathione disulfide, modulating zinc transfer.
  • The role of other cellular ligands in MT function remains less understood.

Purpose of the Study:

  • To investigate the interaction of Adenosine Triphosphate (ATP) with metallothionein (MT).
  • To determine how ATP binding affects MT's zinc transfer capabilities and reactivity.
  • To explore the influence of cellular redox and energy states on MT function.

Main Methods:

  • Characterization of ATP-MT complex formation using binding constants (Kd).
  • Assessing zinc transfer to apo-sorbitol dehydrogenase.
  • Monitoring thiol-disulfide interchange with Ellman's reagent.

Related Experiment Videos

  • Investigating the effect of lysyl carbamoylation on ATP binding.

    • Main Results:

    • ATP forms a 1:1 complex with MT, enhancing zinc transfer and thiol-disulfide interchange.
    • GTP shows similar effects to ATP, while other nucleotides do not bind as strongly.
    • Lysine residues on MT are crucial for ATP binding.
    • Glutathione disulfide enhances ATP binding to MT, whereas GSH decreases it.

    Conclusions:

    • MT actively participates in cellular zinc distribution, not just acting as a buffer.
    • ATP and cellular redox state (GSH/glutathione disulfide) are critical effectors of MT function.
    • MT's interaction with ATP suggests it plays a role in cellular energy metabolism and zinc homeostasis.