Functional significance of AtHMA4 C-terminal domain in planta.

Enhancing the upward translocation of heavy metals such as Zn from root to shoot through genetic engineering has potential for biofortification and phytoremediation. This study examined the contribution of the heavy metal-transporting ATPase, AtHMA4, to the shoot ionomic profile of soil-grown plants...

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Main Authors: Rebecca F Mills, Billy Valdes, Michael Duke, Kerry A Peaston, Brett Lahner, David E Salt, Lorraine E Williams
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2010-10-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC2958113?pdf=render
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author Rebecca F Mills
Billy Valdes
Michael Duke
Kerry A Peaston
Brett Lahner
David E Salt
Lorraine E Williams
author_facet Rebecca F Mills
Billy Valdes
Michael Duke
Kerry A Peaston
Brett Lahner
David E Salt
Lorraine E Williams
author_sort Rebecca F Mills
collection DOAJ
description Enhancing the upward translocation of heavy metals such as Zn from root to shoot through genetic engineering has potential for biofortification and phytoremediation. This study examined the contribution of the heavy metal-transporting ATPase, AtHMA4, to the shoot ionomic profile of soil-grown plants, and investigated the importance of the C-terminal domain in the functioning of this transporter.The Arabidopsis hma2 hma4 mutant has a stunted phenotype and a distinctive ionomic profile, with low shoot levels of Zn, Cd, Co, K and Rb, and high shoot Cu. Expression of AtHMA4 (AtHMA4-FL) under the CaMV-35S promoter partially rescued the stunted phenotype of hma2 hma4; rosette diameter returned to wild-type levels in the majority of lines and bolts were also produced, although the average bolt height was not restored completely. AtHMA4-FL expression rescued Co, K, Rb and Cu to wild-type levels, and partially returned Cd and Zn levels (83% and 28% of wild type respectively). In contrast, expression of AtHMA4-trunc (without the C-terminal region) in hma2 hma4 only partially restored the rosette diameter in two of five lines and bolt production was not rescued. There was no significant effect on the shoot ionomic profile, apart from Cd, which was increased to 41% of wild-type levels. When the AtHMA4 C-terminal domain (AtHMA4-C-term) was expressed in hma2 hma4 it had no marked effect. When expressed in yeast, AtHMA4-C-term and AtHMA4-trunc conferred greater Cd and Zn tolerance than AtHMA4-FL.The ionome of the hma2 hma4 mutant differs markedly from wt plants. The functional relevance of domains of AtHMA4 in planta can be explored by complementing this mutant. AtHMA4-FL is more effective in restoring shoot metal accumulation in this mutant than a C-terminally truncated version of the pump, indicating that the C-terminal domain is important in the functioning of AtHMA4 in planta.
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spelling doaj.art-e0ad6a4fc243473c993da503db55951b2022-12-22T03:07:43ZengPublic Library of Science (PLoS)PLoS ONE1932-62032010-10-01510e1338810.1371/journal.pone.0013388Functional significance of AtHMA4 C-terminal domain in planta.Rebecca F MillsBilly ValdesMichael DukeKerry A PeastonBrett LahnerDavid E SaltLorraine E WilliamsEnhancing the upward translocation of heavy metals such as Zn from root to shoot through genetic engineering has potential for biofortification and phytoremediation. This study examined the contribution of the heavy metal-transporting ATPase, AtHMA4, to the shoot ionomic profile of soil-grown plants, and investigated the importance of the C-terminal domain in the functioning of this transporter.The Arabidopsis hma2 hma4 mutant has a stunted phenotype and a distinctive ionomic profile, with low shoot levels of Zn, Cd, Co, K and Rb, and high shoot Cu. Expression of AtHMA4 (AtHMA4-FL) under the CaMV-35S promoter partially rescued the stunted phenotype of hma2 hma4; rosette diameter returned to wild-type levels in the majority of lines and bolts were also produced, although the average bolt height was not restored completely. AtHMA4-FL expression rescued Co, K, Rb and Cu to wild-type levels, and partially returned Cd and Zn levels (83% and 28% of wild type respectively). In contrast, expression of AtHMA4-trunc (without the C-terminal region) in hma2 hma4 only partially restored the rosette diameter in two of five lines and bolt production was not rescued. There was no significant effect on the shoot ionomic profile, apart from Cd, which was increased to 41% of wild-type levels. When the AtHMA4 C-terminal domain (AtHMA4-C-term) was expressed in hma2 hma4 it had no marked effect. When expressed in yeast, AtHMA4-C-term and AtHMA4-trunc conferred greater Cd and Zn tolerance than AtHMA4-FL.The ionome of the hma2 hma4 mutant differs markedly from wt plants. The functional relevance of domains of AtHMA4 in planta can be explored by complementing this mutant. AtHMA4-FL is more effective in restoring shoot metal accumulation in this mutant than a C-terminally truncated version of the pump, indicating that the C-terminal domain is important in the functioning of AtHMA4 in planta.http://europepmc.org/articles/PMC2958113?pdf=render
spellingShingle Rebecca F Mills
Billy Valdes
Michael Duke
Kerry A Peaston
Brett Lahner
David E Salt
Lorraine E Williams
Functional significance of AtHMA4 C-terminal domain in planta.
PLoS ONE
title Functional significance of AtHMA4 C-terminal domain in planta.
title_full Functional significance of AtHMA4 C-terminal domain in planta.
title_fullStr Functional significance of AtHMA4 C-terminal domain in planta.
title_full_unstemmed Functional significance of AtHMA4 C-terminal domain in planta.
title_short Functional significance of AtHMA4 C-terminal domain in planta.
title_sort functional significance of athma4 c terminal domain in planta
url http://europepmc.org/articles/PMC2958113?pdf=render
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