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Distinct metal binding configurations in ACE1

C T Dameron1, G N George, P Arnold

  • 1University of Utah Medical Center, Salt Lake City 84132.

Biochemistry
|July 20, 1993
PubMed
Summary
This summary is machine-generated.

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The ACE1 protein binds metal ions similarly to metallothionein (MT). Its copper-bound form specifically interacts with DNA, suggesting MT-metal clusters are good models for ACE1's metal center.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • The ACE1 protein regulates metal-induced expression of metallothionein (MT) genes in Saccharomyces cerevisiae.
  • ACE1 shares structural similarities with MT proteins in metal complex formation.

Purpose of the Study:

  • To investigate the metal-binding properties of ACE1 and compare them to yeast metallothionein.
  • To elucidate the structural basis for ACE1's DNA-binding specificity with copper ions.

Main Methods:

  • Spectroscopic studies (UV-Vis, EXAFS) were used to analyze metal-ACE1 complexes.
  • Coordination chemistry of ACE1 with various metal ions (Cu(I), Cd(II), Zn(II), Co(II)) was investigated.
  • Comparison of metal-binding stoichiometry and coordination geometry between ACE1 and MT.

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Main Results:

  • ACE1 binds Cd(II) and Cu(I) ions distinctly; only the Cu(I) form binds DNA with high affinity.
  • Cu(I) ions form polymetallic Cu(I)-thiolate clusters in ACE1, mimicking Cu-metallothionein.
  • Divalent ions bind to ACE1 and MT with similar maximal stoichiometry (approx. 4 mol equiv).
  • Spectroscopic and EXAFS analyses revealed tetrahedral coordination geometry for Cd(II) and Co(II) in ACE1, similar to MT.

Conclusions:

  • Metal binding in ACE1 closely resembles that in yeast metallothionein.
  • MT-metal clusters serve as effective structural models for the metal center of ACE1.
  • The distinct binding of Cu(I) by ACE1 is crucial for its DNA-binding function in gene regulation.