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Updated: Jun 3, 2025

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
The petunia heavy metal P-type ATPase PhHMA5II1 interacts with copper chaperons and regulate Cu detoxification
Liru Pan1, Ruiling Li1, Jinglei Wu1
1School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai, 200240, China.
Key Message:
An endoplasmic reticulum-localized Cu transporter, PhHMA5II1, interacts with copper chaperones and plays an important role in Cu detoxification in petunia. Copper (Cu) is an essential element for plant growth but toxic when present in excess. In this study we present the functional characterization of a petunia (Petunia hybrida) P1B-type heavy-metal ATPases (HMAs), PhHMA5II1. Heterologous expression of PhHMA5II1 in yeast (Saccharomyces cerevisiae) showed Cu transport activity. The expression of PhHMA5II1 in roots and shoots was unaffected by excess Cu. CRISPR/Cas9-edited mutant lines and PhHMA5II1 overexpressing transgenic plants were generated to investigate the functions of PhHMA5II1 in petunia. The PhHMA5II1 knockout mutant was hypersensitive to excess Cu and accumulated more Cu in roots compared to wild-type petunia. Overexpression of PhHMA5II1 enhanced Cu tolerance and reduced Cu accumulation in roots. Furthermore, PhHMA5II1 localized in endoplasmic reticulum, and the localization was unaffected by excess Cu. Yeast two-hybrid experiments and bimolecular fluorescence complementation assays demonstrate that PhHMA5II1 interact with petunia copper chaperons, PhATX1 and PhCCH. Finally, RNA-sequencing revealed that knockout PhHMA5II1 affected the expression of genes involved in cell-wall organization, copper ion homeostasis, and response to oxidative stress. Taken together, PhHMA5II1 plays an important role in Cu detoxification in petunia.
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