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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Published in: | Plant direct Vol. 7; no. 5; pp. e495 - n/a |
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01-05-2023
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Abstract | 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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AbstractList | 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. 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. Abstract 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. 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.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. Manganese (Mn) is an essential micronutrient for plant growth but becomes toxic when present in excess. A number of 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 -Golgi and plays a major role in response to Mn deficiency with severe effects seen in under low Mn supply. ECA3 plays a minor role in Mn-toxicity tolerance, but only when the -Golgi-localized MTP11 is non-functional. We also use mutants and overexpressors to determine the relative contributions of MTP members to Mn homeostasis. The -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 mutants. MTP8 and MTP10 confer greater Mn-toxicity resistance to the 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. |
Author | Garcia‐Becerra, Tania Henbest, Kate C. Peaston, Kerry A. Farthing, Emily C. Williams, Lorraine E. |
AuthorAffiliation | 1 School of Biological Sciences University of Southampton Southampton Hampshire UK |
AuthorAffiliation_xml | – name: 1 School of Biological Sciences University of Southampton Southampton Hampshire UK |
Author_xml | – sequence: 1 givenname: Emily C. surname: Farthing fullname: Farthing, Emily C. organization: University of Southampton – sequence: 2 givenname: Kate C. surname: Henbest fullname: Henbest, Kate C. organization: University of Southampton – sequence: 3 givenname: Tania surname: Garcia‐Becerra fullname: Garcia‐Becerra, Tania organization: University of Southampton – sequence: 4 givenname: Kerry A. surname: Peaston fullname: Peaston, Kerry A. organization: University of Southampton – sequence: 5 givenname: Lorraine E. orcidid: 0000-0003-1373-8699 surname: Williams fullname: Williams, Lorraine E. email: lew@soton.ac.uk organization: University of Southampton |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/37228331$$D View this record in MEDLINE/PubMed |
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Keywords | P‐type ATPase cation diffusion facilitator (CDF) metal tolerance protein (MTP) heavy metal natural resistance‐associated macrophage protein (NRAMP) transport manganese |
Language | English |
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Snippet | 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... Manganese (Mn) is an essential micronutrient for plant growth but becomes toxic when present in excess. A number of proteins are involved in Mn transport... 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... Abstract Manganese (Mn) is an essential micronutrient for plant growth but becomes toxic when present in excess. A number of Arabidopsis proteins are involved... |
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SubjectTerms | 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 |
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Title | Dissecting the relative contribution of ECA3 and group 8/9 cation diffusion facilitators to manganese homeostasis in Arabidopsis thaliana |
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