The University of Southampton
University of Southampton Institutional Repository

The plant P-1B-type ATPase AtHMA4 transports Zn and Cd and plays a role in detoxification of transition metals supplied at elevated levels

The plant P-1B-type ATPase AtHMA4 transports Zn and Cd and plays a role in detoxification of transition metals supplied at elevated levels
The plant P-1B-type ATPase AtHMA4 transports Zn and Cd and plays a role in detoxification of transition metals supplied at elevated levels
The transition metal Zn is essential for many physiological processes in plants, yet at elevated concentrations this, and the related non-essential metal Cd, can be toxic. Arabidopsis thaliana HMA4, belonging to the Type P1B subfamily of P-type ATPases, has recently been implicated in Zn nutrition, having a role in root to shoot Zn translocation. Using Arabidopsis insertional mutants, it is shown here that disruption of AtHMA4 function also results in increased sensitivity to elevated levels of Cd and Zn, suggesting that AtHMA4 serves an important role in metal detoxification at higher metal concentrations. AtHMA4 and a truncated form lacking the last 457 amino acids both confer Cd and Zn resistance to yeast but a mutant version of the full-length AtHMA4 (AtHMA4-C357G) does not; this demonstrates that the C-terminal region is not essential for this function. Evidence is presented that AtHMA4 functions as an efflux pump.
heterologous yeast expression, metal homeostasis, insertional mutant, P-type ATPase, transition metal transport, arabidopsis thaliana
0014-5793
783-791
Mills, Rebecca F.
dec4afc8-be3b-4517-9038-c3c3e8b71b35
Francini, Alessandra
274980c2-8487-4150-9331-b9f21f2935a7
Ferreira da Rocha, Pedro S.C.
03cfcd53-8d10-4cf3-aa90-94315f1c599f
Baccarini, Paul J.
306c592f-8866-4907-b4ae-e888ff80a4ce
Aylett, Melissa
a05d3031-e86c-4b5a-a0f0-50fce0b6ee89
Krijger, Gerard C.
5b7cdf7f-ad85-4db7-94c0-38242eb06ac4
Williams, Lorraine E.
79ee1856-3732-492b-8ac5-239749c85d9e
Mills, Rebecca F.
dec4afc8-be3b-4517-9038-c3c3e8b71b35
Francini, Alessandra
274980c2-8487-4150-9331-b9f21f2935a7
Ferreira da Rocha, Pedro S.C.
03cfcd53-8d10-4cf3-aa90-94315f1c599f
Baccarini, Paul J.
306c592f-8866-4907-b4ae-e888ff80a4ce
Aylett, Melissa
a05d3031-e86c-4b5a-a0f0-50fce0b6ee89
Krijger, Gerard C.
5b7cdf7f-ad85-4db7-94c0-38242eb06ac4
Williams, Lorraine E.
79ee1856-3732-492b-8ac5-239749c85d9e

Mills, Rebecca F., Francini, Alessandra, Ferreira da Rocha, Pedro S.C., Baccarini, Paul J., Aylett, Melissa, Krijger, Gerard C. and Williams, Lorraine E. (2005) The plant P-1B-type ATPase AtHMA4 transports Zn and Cd and plays a role in detoxification of transition metals supplied at elevated levels. FEBS Letters, 579 (3), 783-791. (doi:10.1016/j.febslet.2004.12.040).

Record type: Article

Abstract

The transition metal Zn is essential for many physiological processes in plants, yet at elevated concentrations this, and the related non-essential metal Cd, can be toxic. Arabidopsis thaliana HMA4, belonging to the Type P1B subfamily of P-type ATPases, has recently been implicated in Zn nutrition, having a role in root to shoot Zn translocation. Using Arabidopsis insertional mutants, it is shown here that disruption of AtHMA4 function also results in increased sensitivity to elevated levels of Cd and Zn, suggesting that AtHMA4 serves an important role in metal detoxification at higher metal concentrations. AtHMA4 and a truncated form lacking the last 457 amino acids both confer Cd and Zn resistance to yeast but a mutant version of the full-length AtHMA4 (AtHMA4-C357G) does not; this demonstrates that the C-terminal region is not essential for this function. Evidence is presented that AtHMA4 functions as an efflux pump.

Text
Millsetal2005(3).pdf - Other
Restricted to Registered users only
Download (1MB)
Request a copy

More information

Submitted date: 3 August 2004
Published date: 31 January 2005
Keywords: heterologous yeast expression, metal homeostasis, insertional mutant, P-type ATPase, transition metal transport, arabidopsis thaliana
Organisations: Biological Sciences

Identifiers

Local EPrints ID: 35538
URI: http://eprints.soton.ac.uk/id/eprint/35538
ISSN: 0014-5793
PURE UUID: 01d7ccb0-b300-4c4f-abc6-f4b1e36170b1

Catalogue record

Date deposited: 18 May 2006
Last modified: 15 Mar 2024 07:52

Export record

Altmetrics

Contributors

Author: Rebecca F. Mills
Author: Alessandra Francini
Author: Pedro S.C. Ferreira da Rocha
Author: Paul J. Baccarini
Author: Melissa Aylett
Author: Gerard C. Krijger

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×