Dissecting the relative contribution of ECA3 and group 8/9 cation diffusion facilitators to manganese homeostasis in Arabidopsis thaliana

Dissecting the relative contribution of ECA3 and group 8/9 cation diffusion facilitators to manganese homeostasis in Arabidopsis thaliana

Manganese (Mn) is an essential micronutrient for plant growth but becomes toxic when present in excess. A number of Arabidopsis proteins are involved in Mn transport including ECA3, MTPs, and NRAMPs; however, their relative contributions to Mn homeostasis remain to be demonstrated. A major focus her...

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Bibliographic Details
Published in:Plant direct Vol. 7; no. 5; pp. e495 - n/a
Main Authors: Farthing, Emily C., Henbest, Kate C., Garcia‐Becerra, Tania, Peaston, Kerry A., Williams, Lorraine E.
Format: Journal Article
Language:English
Published: England John Wiley & Sons, Inc 01-05-2023
John Wiley and Sons Inc
Wiley
Subjects:
Agricultural production
cation diffusion facilitator (CDF)
Chloroplasts
Efficiency
Endoplasmic reticulum
Golgi apparatus
heavy metal
Homeostasis
Localization
Manganese
metal tolerance protein (MTP)
Mutants
natural resistance‐associated macrophage protein (NRAMP)
Original Research
Photosynthesis
Proteins
P‐type ATPase
Roles
Toxicity
Toxicity tolerance
transport
P‐type ATPase
cation diffusion facilitator (CDF)
metal tolerance protein (MTP)
heavy metal
natural resistance‐associated macrophage protein (NRAMP)
transport
manganese
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Summary:Manganese (Mn) is an essential micronutrient for plant growth but becomes toxic when present in excess. A number of Arabidopsis proteins are involved in Mn transport including ECA3, MTPs, and NRAMPs; however, their relative contributions to Mn homeostasis remain to be demonstrated. A major focus here was to clarify the importance of ECA3 in responding to Mn deficiency and toxicity using a range of mutants. We show that ECA3 localizes to the trans‐Golgi and plays a major role in response to Mn deficiency with severe effects seen in eca3 nramp1 nramp2 under low Mn supply. ECA3 plays a minor role in Mn‐toxicity tolerance, but only when the cis‐Golgi‐localized MTP11 is non‐functional. We also use mutants and overexpressors to determine the relative contributions of MTP members to Mn homeostasis. The trans‐Golgi‐localized MTP10 plays a role in Mn‐toxicity tolerance, but this is only revealed in mutants when MTP8 and MTP11 are non‐functional and when overexpressed in mtp11 mutants. MTP8 and MTP10 confer greater Mn‐toxicity resistance to the pmr1 yeast mutant than MTP11, and an important role for the first aspartate in the fifth transmembrane domain DxxxD motif is demonstrated. Overall, new insight into the relative influence of key transporters in Mn homeostasis is provided.
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ISSN:2475-4455
2475-4455
DOI:10.1002/pld3.495