A cloned prokaryotic Cd2+ P-type ATPase increases yeast sensitivity to Cd2+.

Abstract CadA, the P1-type ATPase involved in Listeria monocytogenes resistance to Cd 2+ , was expressed in Saccharomyces cerevisiae and did just the opposite to what was expected, as it strikingly decreased the Cd 2+ tolerance of these cells. Yeast cells expressing the non-functional mutant Asp 398 Ala could grow on selective medium containing up to 100 μM Cd 2+ , whereas those expressing the functional protein could not grow in the presence of 1 μM Cd 2+ . The CadA–GFP fusion protein was localized in the endoplasmic reticulum membrane, suggesting that yeast hyper-sensitivity was due to Cd 2+ accumulation in the reticulum lumen. CadA is also known to transport Zn 2+ , but Zn 2+ did not protect the cells against Cd 2+ poisoning. In the presence of 10 μM Cd 2+ , transformed yeasts survived by rapid loss of their expression vector.