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Papers In Press, published online ahead of print May 14, 2002
Environmental Toxicology, University of California, Santa Cruz, CA 95064
Corresponding Author: zhu{at}biology.ucsc.edu
Copper ion uptake must be regulated to avoid both deficiency and excess, because its essential yet toxic biological nature depends on the concentration. Yeast copper uptake is controlled at both the transcriptional and posttranslational levels. The transcription of CTR1 and CTR3, encoding high affinity copper ion transporters, is regulated by the copper ion-sensing transcription factor Mac1p through the cis-acting copper responsive elements (CuRE) in CTR1 and CTR3 promoters. The Ctr1p is known to undergo degradation in cells exposed to high copper levels. We report that the Mac1p is also required for Ctr1p degradation responding to copper ions. Mutations within a conserved copper ion-binding motif, the “Cu-fist’ in the Mac1p DNA-binding domain, cause defects in Ctr1p turnover; mutations within a metal ion-binding motif REP-III located in the cytosolic domain of Ctr1p also impede the turnover. Furthermore, we show that the Mac1p limits intracellular copper accumulation likely by controlling Ctr1p degradation. These data indicate that the Mac1p not only regulates the transcription of CTR1, but also controls the posttranslational degradation of Ctr1p as well. The findings have uncovered an unprecedented mechanism by which a transcription factor not only regulates its target gene transcription but also controls the degradation of its target gene product.
J. Biol. Chem, 10.1074/jbc.C200203200
Submitted on April 3, 2002
Revised on May 10, 2002
Accepted on May 14, 2002
Copper ion-sensing transcription factor Mac1p post-translationally controls the degradation of its target gene product Ctr1p
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