Reference : di-Cysteine motifs in the C-terminus of plant HMA4 proteins confer nanomolar affinity...
Scientific journals : Article
Life sciences : Phytobiology (plant sciences, forestry, mycology...)
http://hdl.handle.net/2268/230719
di-Cysteine motifs in the C-terminus of plant HMA4 proteins confer nanomolar affinity for zinc and are essential for HMA4 function in vivo.
English
Lekeux, Gilles [Université de Liège - ULiège > Département des sciences de la vie > Centre d'ingénierie des protéines >]
Laurent, Clémentine [Université de Liège > Département des sciences de la vie > Macromolécules biologiques >]
Joris, Marine mailto [> >]
Jadoul, Alice [> >]
Jiang, Dan [> >]
Bosman, Bernard [Université de Liège - ULiège > Département de Biologie, Ecologie et Evolution > Ecologie végétale et microbienne >]
Carnol, Monique [Université de Liège - ULiège > Département de Biologie, Ecologie et Evolution > Ecologie végétale et microbienne >]
Motte, Patrick [Université de Liège - ULiège > Département des sciences de la vie > Génomique fonctionnelle et imagerie moléculaire végétale >]
Xiao, Zhiguang [> >]
Galleni, Moreno mailto [Université de Liège - ULiège > Département des sciences de la vie > Macromolécules biologiques >]
Hanikenne, Marc mailto [Université de Liège - ULiège > Département des sciences de la vie > Génomique fonctionnelle et imagerie moléculaire végétale >]
2018
Journal of Experimental Botany
69
22
5547-5560
Yes (verified by ORBi)
International
0022-0957
1460-2431
United Kingdom
[en] 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.
http://hdl.handle.net/2268/230719
10.1093/jxb/ery311

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