TY - JOUR
T1 - Copper redox chemistry of plant frataxins
AU - Sánchez, Manu
AU - Palacios, Òscar
AU - Buchensky, Celeste
AU - Sabio, Laura
AU - Gomez-Casati, Diego Fabian
AU - Pagani, Maria Ayelen
AU - Capdevila, Mercè
AU - Atrian, Silvia
AU - Dominguez-Vera, Jose M.
N1 - Publisher Copyright:
© 2017 Elsevier Inc.
PY - 2018/3/1
Y1 - 2018/3/1
N2 - The presence of a conserved cysteine residue in the C-terminal amino acid sequences of plant frataxins differentiates these frataxins from those of other kingdoms and may be key in frataxin assembly and function. We report a full study on the ability of Arabidopsis (AtFH) and Zea mays (ZmFH-1 and ZmFH-2) frataxins to assemble into disulfide-bridged dimers by copper-driven oxidation and to revert to monomers by chemical reduction. We monitored the redox assembly-disassembly process by electrospray ionization mass spectrometry, electrophoresis, UV–Vis spectroscopy, and fluorescence measurements. We conclude that plant frataxins AtFH, ZmFH-1 and ZmFH-2 are oxidized by Cu2 + and exhibit redox cysteine monomer – cystine dimer interexchange. Interestingly, the tendency to interconvert is not the same for each protein. Through yeast phenotypic rescue experiments, we show that plant frataxins are important for plant survival under conditions of excess copper, indicating that these proteins might be involved in copper metabolism.
AB - The presence of a conserved cysteine residue in the C-terminal amino acid sequences of plant frataxins differentiates these frataxins from those of other kingdoms and may be key in frataxin assembly and function. We report a full study on the ability of Arabidopsis (AtFH) and Zea mays (ZmFH-1 and ZmFH-2) frataxins to assemble into disulfide-bridged dimers by copper-driven oxidation and to revert to monomers by chemical reduction. We monitored the redox assembly-disassembly process by electrospray ionization mass spectrometry, electrophoresis, UV–Vis spectroscopy, and fluorescence measurements. We conclude that plant frataxins AtFH, ZmFH-1 and ZmFH-2 are oxidized by Cu2 + and exhibit redox cysteine monomer – cystine dimer interexchange. Interestingly, the tendency to interconvert is not the same for each protein. Through yeast phenotypic rescue experiments, we show that plant frataxins are important for plant survival under conditions of excess copper, indicating that these proteins might be involved in copper metabolism.
KW - Copper chemistry of frataxin
KW - Plant frataxins
KW - Protein assembly
UR - http://www.scopus.com/inward/record.url?scp=85038901930&partnerID=8YFLogxK
U2 - 10.1016/j.jinorgbio.2017.11.020
DO - 10.1016/j.jinorgbio.2017.11.020
M3 - Article
C2 - 29277024
SN - 0162-0134
VL - 180
SP - 135
EP - 140
JO - Journal of Inorganic Biochemistry
JF - Journal of Inorganic Biochemistry
ER -