A combined zinc/cadmium sensor and zinc/cadmium export regulator in a heavy metal pump

Baekgaard, Lone, Mikkelsen, Maria D., Sorensen, Danny M., Hegelund, Josefine N., Persson, Daniel P., Mills, Rebecca F., Yang, Zhang, Husted, Søren, Andersen, Jens Peter, Buch-Pedersen, Morten J., Schjoerring, Jan K., Williams, Lorraine E. and Palmgren, Michael G. (2010) A combined zinc/cadmium sensor and zinc/cadmium export regulator in a heavy metal pump. The Journal of Biological Chemistry, 285 (41), 31243-31252. (doi:10.1074/jbc.M110.111260). (PMID:20650903)

Abstract

Heavy metal pumps (P1B-ATPases) are important for cellular heavy metal homeostasis. AtHMA4, an Arabidopsis thaliana heavy metal pump of importance for plant Zn2+ nutrition, has an extended C-terminal domain containing 13 cysteine pairs and a terminal stretch of 11 histidines. Using a novel size-exclusion chromatography, inductively coupled plasma mass spectrometry approach we report that the C-terminal domain of AtHMA4 is a high affinity Zn2+ and Cd2+ chelator with capacity to bind 10 Zn2+ ions per C terminus. When AtHMA4 is expressed in a Zn2+-sensitive zrc1 cot1 yeast strain, sequential removal of the histidine stretch and the cysteine pairs confers a gradual increase in Zn2+ and Cd2+ tolerance and lowered Zn2+ and Cd2+ content of transformed yeast cells. We conclude that the C-terminal domain of AtHMA4 serves a dual role as Zn2+ and Cd2+ chelator (sensor) and as a regulator of the efficiency of Zn2+ and Cd2+ export. The identification of a post-translational handle on Zn2+ and Cd2+ transport efficiency opens new perspectives for regulation of Zn2+ nutrition and tolerance in eukaryotes.

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