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Characterization and copper binding properties of human COMMD1 (MURR1)
Suree Narindrasorasak1, Prasad Kulkarni, Patrick Deschamps
1Program in Molecular Structure and Function, The Research Institute of the Hospital for Sick Children, and Department of Biochemistry, University of Toronto, Toronto, Canada M5G 1X8.
COMMD1 protein regulates copper metabolism and binds copper ions. A specific product of exon 2, COMMD(61-154), also binds copper, offering insights into copper toxicosis in Bedlington terriers.
Area of Science:
- Biochemistry
- Molecular Biology
- Genetics
Background:
- COMMD1 (copper metabolism gene MURR1 domain) protein family inhibits NF-kappaB.
- COMMD1 is linked to copper metabolism regulation, with exon 2 deletions causing copper toxicosis in Bedlington terriers.
Purpose of the Study:
- Characterize the copper binding properties of purified recombinant human COMMD1.
- Investigate the role of the COMMD(61-154) protein, a product of exon 2, in copper binding and homeostasis.
Main Methods:
- Native-PAGE, EPR, UV-visible absorption, and fluorescence spectroscopies.
- DEPC modification of histidines, MALDI MS mapping, and MS/MS sequencing.
- Site-directed mutagenesis and fluorescence studies.
Main Results:
- COMMD1 specifically binds copper as Cu(II) with 1:1 stoichiometry and does not bind other divalent metals.
- The COMMD(61-154) protein also binds Cu(II) with 1:1 stoichiometry per monomer.
- Cu(II) binding involves His residues (H101, H134) and M110.
Conclusions:
- COMMD1 and its exon 2 product COMMD(61-154) directly bind copper.
- These findings elucidate the function of COMMD1 and COMMD(61-154) in regulating copper homeostasis.
- Provides molecular insights into copper toxicosis linked to COMMD1 exon 2 deletions.
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