Biochemical and Biophysical Research Communications
Copper-dependent interaction of glutaredoxin with the N termini of the copper-ATPases (ATP7A and ATP7B) defective in Menkes and Wilson diseases☆
Section snippets
Materials and methods
Bacterial, yeast, and mammalian cell strains. Escherichia coli strain DH10B (F−, mcrA, Δ(mrr-hsdRMS-mcrBC), Φ80lacZΔM15, ΔlacX74, deoR, recA1, araD, Δ(ara,leu)7697, galU, galK, rpsL, endA1, nupG) was used for the maintenance and propagation of plasmids, and grown in Luria–Bertani medium (LB) (0.1% (w/v) bactotryptone (Difco), 0.05% (w/v) yeast extract (Difco), and 0.1% (w/v) NaCl) containing 100 μg/ml ampicillin for plasmid selection. Saccharomyces cerevisiae strain YGH1 (ura3-25 his3-200
Screening of a human liver cDNA library for interacting partners of the ATP7B N-terminal domain
A human liver cDNA library was previously screened with the entire N-terminal domain of ATP7B from amino acid 1 to 657 [17]. Of 36 different cDNAs identified to encode interacting proteins one encoded the full-length GRX1 protein. Based on the presence of the conserved copper-binding motif, CxxC in GRX1, the well-established role of GRX1 in regulating the redox status of protein thiols, in particular its role in reducing intramolecular disulphide bonds and in deglutathionylating cysteinyl
Discussion
The identification of interacting partners of the copper ATPases is important in helping to explain the molecular and biochemical basis for disease-causing mutations and for full understanding of the complex mechanisms involved in copper homeostasis. We have identified an additional interacting partner of both ATP7A and ATP7B. GRX1 was chosen as a candidate likely to be implicated in regulating ATPase activity based on the presence of the conserved copper-binding CxxC motif within its amino
Acknowledgments
We thank Jonathan Gitlin (Washington University School of Medicine, St. Louis, Missouri) for the use of the wild-type ATP7B construct, Diane Cox and John Forbes (University of Alberta, Edmonton, Alberta) for supplying the plasmid constructs containing the ATP7B mutations and deletions, and Hamsa Puthalakath (The Walter & Eliza Hall Institute, Victoria) for providing the plasmid encoding Bcl2. We also thank David Clarke (University of Melbourne, Victoria) for helpful scientific discussions. This
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Abbreviations: WD, Wilson disease; MD, Menkes disease; GRX, glutaredoxin; TGN, trans-Golgi network; AD, activation domain; BCS, bathocuproinedisulphonic acid; BD, binding domain; CPRG, chlorophenol red-β-d-galactopyranoside; TCA, trichloroacetic acid; MBS, metal-binding sites; MBD, metal-binding domains.