Metal binding to the N-terminal cytoplasmic domain of the PIB ATPase HMA4 is required for metal transport in Arabidopsis

Plant Molecular Biology
Clémentine LaurentMarc Hanikenne

Abstract

PIB ATPases are metal cation pumps that transport metals across membranes. These proteins possess N- and C-terminal cytoplasmic extensions that contain Cys- and His-rich high affinity metal binding domains, which may be involved in metal sensing, metal ion selectivity and/or in regulation of the pump activity. The PIB ATPase HMA4 (Heavy Metal ATPase 4) plays a central role in metal homeostasis in Arabidopsis thaliana and has a key function in zinc and cadmium hypertolerance and hyperaccumulation in the extremophile plant species Arabidopsis halleri. Here, we examined the function and structure of the N-terminal cytoplasmic metal-binding domain of HMA4. We mutagenized a conserved CCTSE metal-binding motif in the domain and assessed the impact of the mutations on protein function and localization in planta, on metal-binding properties in vitro and on protein structure by Nuclear Magnetic Resonance spectroscopy. The two Cys residues of the motif are essential for the function, but not for localization, of HMA4 in planta, whereas the Glu residue is important but not essential. These residues also determine zinc coordination and affinity. Zinc binding to the N-terminal domain is thus crucial for HMA4 protein function, whereas it is ...Continue Reading

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Citations

Oct 27, 2010·PloS One·Rebecca F MillsLorraine E Williams
Jul 29, 2016·PloS One·Macarena Silva-GuzmanBrian P Dilkes
Oct 6, 2018·The Plant Journal : for Cell and Molecular Biology·Pauliina HalimaaArja I Tervahauta
Apr 28, 2020·The Plant Journal : for Cell and Molecular Biology·Sung Don LimJohn C Cushman
Jun 13, 2020·Frontiers in Plant Science·Stanislaus Antony CeasarMarc Hanikenne
Nov 9, 2020·Journal of Plant Physiology·Yaohui WangZhi Qi
Mar 13, 2021·The Biochemical Journal·Tessa R Young, Zhiguang Xiao

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