AI Article Synopsis

  • - The PIB ATPase heavy metal ATPase 4 (HMA4) is vital for managing zinc levels in Arabidopsis thaliana by facilitating zinc transport from root cells to shoots.
  • - HMA4 is important for zinc accumulation and tolerance to cadmium in Arabidopsis halleri, particularly due to its specific C-terminal extension, which varies between the two species.
  • - Research reveals that certain features of the C-terminal extension, like di-Cys motifs, enhance zinc binding, and while both species' HMA4 proteins perform similar functions, they have slight differences in zinc-binding effectiveness.

Article Abstract

The PIB ATPase heavy metal ATPase 4 (HMA4) has a central role in the zinc homeostasis network of Arabidopsis thaliana. This membrane protein loads metal from the pericycle cells into the xylem in roots, thereby allowing root to shoot metal translocation. Moreover, HMA4 is key for zinc hyperaccumulation as well as zinc and cadmium hypertolerance in the pseudometallophyte Arabidopsis halleri. The plant-specific cytosolic C-terminal extension of HMA4 is rich in putative metal-binding residues and has substantially diverged between A. thaliana and A. halleri. To clarify the function of the domain in both species, protein variants with truncated C-terminal extension, as well as with mutated di-Cys motifs and/or a His-stretch, were functionally characterized. We show that di-Cys motifs, but not the His-stretch, contribute to high affinity zinc binding and function in planta. We suggest that the HMA4 C-terminal extension is at least partly responsible for protein targeting to the plasma membrane. Finally, we reveal that the C-terminal extensions of both A. thaliana and A. halleri HMA4 proteins share similar function, despite marginally different zinc-binding capacity.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6255694PMC
http://dx.doi.org/10.1093/jxb/ery311DOI Listing

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