Human Copper Chaperone Atox1 Translocates to the Nucleus but does not Bind DNA In Vitro.
Artikel i vetenskaplig tidskrift, 2015
After Ctr1-mediated cell uptake, copper (Cu) is transported by the cytoplasmic Cu chaperone Atox1 to P1B type ATPases ATP7A and ATP7B in the Golgi network, for incorporation into Cudependent enzymes. Atox1 is a small 68-residue protein that binds Cu in a conserved CXXC motif; it delivers Cu to target domains in ATP7A/B via direct protein-protein interactions. Specific transcription factors regulating expression of the human Cu transport proteins have not been reported although Atox1 was recently suggested to have dual functionality such that it, in addition to its cytoplasmic chaperone function, acts as a transcription factor in the nucleus. To examine this hypothesis, here we investigated the localization of Atox1 in HeLa cells using fluorescence imaging in combination with in vitro binding experiments to fluorescently labeled DNA duplexes harboring the proposed promotor sequence. We found that whereas Atox1 is present in the nucleus in HeLa cells, it does not bind to DNA in vitro. It appears that Atox1 mediates transcriptional regulation via additional (unknown) proteins.
Fluorescence
metabolism
chemistry
metabolism
Cell Nucleus
chemistry
metabolism
Molecular
DNA
chemistry
chemistry
Metallochaperones
Microscopy
Humans
Copper
metabolism
Models
HeLa Cells
Protein Binding
Författare
Dana Kahra
Umeå universitet
Tanumoy Mondol
Umeå universitet
Moritz S Niemiec
Umeå universitet
Pernilla Wittung Stafshede
Umeå universitet
Protein and peptide letters
1875-5305 (ISSN)
Vol. 22 6 532-8Ämneskategorier (SSIF 2011)
Biokemi och molekylärbiologi
Biologiska vetenskaper
Biofysik
DOI
10.2174/0929866522666150506094546
PubMed
25962064