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

Lone Bækgaard; Maria Dalgaard Mikkelsen; Danny Mollerup Sørensen; Josefine Nymark Hegelund; Daniel Olof Persson; Rebecca F. Mills; Zhang Yang; Søren Husted; Jens Peter Andersen; Morten Jeppe Buch-Pedersen; Jan Kofod Schjørring; Lorraine E. Williams; Michael Broberg Palmgren

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

Lone Bækgaard, Maria Dalgaard Mikkelsen, Danny Mollerup Sørensen, Josefine Nymark Hegelund, Daniel Olof Persson, Rebecca F. Mills, Zhang Yang, Søren Husted, Jens Peter Andersen, Morten Jeppe Buch-Pedersen, Jan Kofod Schjørring, Lorraine E. Williams, Michael Broberg Palmgren

51 Citationer (Scopus)

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 AtHMA4is a high affinity Zn²⁺ and Cd²⁺ chelator with capacity to bind 10 Zn ²⁺ ions per C terminus. When AtHMA4 is expressed in a Zn ²⁺-sensitive zrc1 cot1 yeast strain, sequential removal of the histidine stretch and the cysteine pairs confers a gradual increase in Zn ²⁺ 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 Cd ²⁺ chelator (sensor) and as a regulator of the efficiency of Zn ²⁺ 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.

Originalsprog	Engelsk
Tidsskrift	Journal of Biological Chemistry
Vol/bind	285
Udgave nummer	41
Sider (fra-til)	31243-31252
Antal sider	10
ISSN	0021-9258
Status	Udgivet - 8 okt. 2010

Adgang til dokumentet

http://www.jbc.org/content/suppl/2010/07/22/M110.111260.DC1.html

Citationsformater

Bækgaard, L., Mikkelsen, M. D., Sørensen, D. M., Hegelund, J. N., Persson, D. O., Mills, R. F., Yang, Z., Husted, S., Andersen, J. P., Buch-Pedersen, M. J., Schjørring, J. K., Williams, L. E., & Palmgren, M. B. (2010). A combined zinc/cadmium sensor and zinc/cadmium export regulator in a heavy metal pump. Journal of Biological Chemistry, 285(41), 31243-31252. http://www.jbc.org/content/suppl/2010/07/22/M110.111260.DC1.html

Bækgaard, L, Mikkelsen, MD, Sørensen, DM, Hegelund, JN, Persson, DO, Mills, RF, Yang, Z , Husted, S, Andersen, JP, Buch-Pedersen, MJ, Schjørring, JK, Williams, LE & Palmgren, MB 2010, 'A combined zinc/cadmium sensor and zinc/cadmium export regulator in a heavy metal pump', Journal of Biological Chemistry, bind 285, nr. 41, s. 31243-31252. <http://www.jbc.org/content/suppl/2010/07/22/M110.111260.DC1.html>

@article{c9d4a720d2b311df825b000ea68e967b,

title = "A combined zinc/cadmium sensor and zinc/cadmium export regulator in a heavy metal pump",

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 AtHMA4is a high affinity Zn2+ and Cd2+ chelator with capacity to bind 10 Zn 2+ ions per C terminus. When AtHMA4 is expressed in a Zn 2+-sensitive zrc1 cot1 yeast strain, sequential removal of the histidine stretch and the cysteine pairs confers a gradual increase in Zn 2+ 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 Cd 2+ chelator (sensor) and as a regulator of the efficiency of Zn 2+ 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.",

author = "Lone B{\ae}kgaard and Mikkelsen, {Maria Dalgaard} and S{\o}rensen, {Danny Mollerup} and Hegelund, {Josefine Nymark} and Persson, {Daniel Olof} and Mills, {Rebecca F.} and Zhang Yang and S{\o}ren Husted and Andersen, {Jens Peter} and Buch-Pedersen, {Morten Jeppe} and Schj{\o}rring, {Jan Kofod} and Williams, {Lorraine E.} and Palmgren, {Michael Broberg}",

year = "2010",

month = oct,

day = "8",

language = "English",

volume = "285",

pages = "31243--31252",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology, Inc.",

number = "41",

}

TY - JOUR

T1 - A combined zinc/cadmium sensor and zinc/cadmium export regulator in a heavy metal pump

AU - Bækgaard, Lone

AU - Mikkelsen, Maria Dalgaard

AU - Sørensen, Danny Mollerup

AU - Hegelund, Josefine Nymark

AU - Persson, Daniel Olof

AU - Mills, Rebecca F.

AU - Yang, Zhang

AU - Husted, Søren

AU - Andersen, Jens Peter

AU - Buch-Pedersen, Morten Jeppe

AU - Schjørring, Jan Kofod

AU - Williams, Lorraine E.

AU - Palmgren, Michael Broberg

PY - 2010/10/8

Y1 - 2010/10/8

N2 - 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 AtHMA4is a high affinity Zn2+ and Cd2+ chelator with capacity to bind 10 Zn 2+ ions per C terminus. When AtHMA4 is expressed in a Zn 2+-sensitive zrc1 cot1 yeast strain, sequential removal of the histidine stretch and the cysteine pairs confers a gradual increase in Zn 2+ 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 Cd 2+ chelator (sensor) and as a regulator of the efficiency of Zn 2+ 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.

AB - 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 AtHMA4is a high affinity Zn2+ and Cd2+ chelator with capacity to bind 10 Zn 2+ ions per C terminus. When AtHMA4 is expressed in a Zn 2+-sensitive zrc1 cot1 yeast strain, sequential removal of the histidine stretch and the cysteine pairs confers a gradual increase in Zn 2+ 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 Cd 2+ chelator (sensor) and as a regulator of the efficiency of Zn 2+ 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.

M3 - Journal article

SN - 0021-9258

VL - 285

SP - 31243

EP - 31252

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 41

ER -

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

Abstract

Adgang til dokumentet

Fingeraftryk

Citationsformater