Cd2+ binds to Atx1 and affects the physical interaction between Atx1 and Ccc2 in Saccharomyces cerevisiae.
The ATX1 deletion strain of Saccharomyces cerevisiae is more resistant to Cd(2+) than the wild-type. To investigate the function of Atx1 in Cd(2+) toxicity, we used a metal-binding assay to study the interaction between Atx1 and Cd(2+) in vitro. Using circular dichroism and two-hybrid analyses, we found that Atx1 can bind Cd(2+) specifically and that Cd(2+) binding to Atx1 affects the physical interaction between Atx1 and Ccc2. These results imply that Atx1 delivers Cd(2+) to Ccc2 and that this delivery is, at least in part, responsible for Cd(2+) toxicity in S. cerevisiae.
School of Life Sciences and Biotechnology, Korea University, Anam-dong, Sungbuk-gu, Seoul, Republic of Korea.
Dong-Hyuk
DH
Heo
In-Joon
IJ
Baek
Hyun-Jun
HJ
Kang
Ji-Hyun
JH
Kim
Miwha
M
Chang
Chang-Min
CM
Kang
Cheol-Won
CW
Yun
D002104:Cadmium / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D027682:Cation Transport Proteins / Q000378:metabolism*; D002413:Cations, Divalent / Q000378:metabolism*; D002942:Circular Dichroism; D000079922:Copper Transport Proteins; D011485:Protein Binding; D025941:Protein Interaction Mapping; D012441:Saccharomyces cerevisiae / Q000187:drug effects*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D020798:Two-Hybrid System Techniques
C093341:ATX1 protein, S cerevisiae; C092974:CCC2 protein, S cerevisiae; D002352:Carrier Proteins; D027682:Cation Transport Proteins; D002413:Cations, Divalent; D000079922:Copper Transport Proteins; D029701:Saccharomyces cerevisiae Proteins; D002104:Cadmium