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Proteomic survey of copper‐binding proteins in Arabidopsis roots by immobilized metal affinity chromatography and mass spectrometry
Author(s) -
Kung ChengChe S.,
Huang WeiNing,
Huang YanChen,
Yeh KuoChen
Publication year - 2006
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200500108
Subject(s) - proteome , copper , arabidopsis , chemistry , affinity chromatography , glutathione , biochemistry , chelation , proteomics , cysteine , mass spectrometry , metalloprotein , metabolism , chromatography , enzyme , inorganic chemistry , organic chemistry , mutant , gene
To plants, copper is vitally essential at low concentrations but extremely toxic at elevated concentrations. Plants have evolved a suite of mechanisms that modulate the uptake, distribution, and utilization of copper ions. These mechanisms require copper‐interacting proteins for transporting, chelating, and sequestrating copper ions. In this study, we have systematically screened for copper‐interacting proteins in Arabidopsis roots via copper‐immobilized metal affinity chromatography (Cu‐IMAC). We also compared Arabidopsis root metalloproteomes with affinity to Cu‐IMAC and Zn‐IMAC. From the identities of 38 protein spots with affinity to Cu‐IMAC, 35 unique proteins were identified. Functional classification of these proteins includes redox/hydrolytic reactions, amino acid metabolism, glutathione metabolism, phosphorylation, translation machinery, membrane‐associated proteins, and vegetative storage proteins. Potential copper‐interacting motifs were predicted and scored. Six candidate motifs, H‐(X) 5 ‐H, H‐(X) 7 ‐H, H‐(X) 12 ‐H, H‐(X) 6 ‐M, M‐(X) 7 ‐H, and H‐(X) 3 ‐C, are present in Cu‐IMAC‐isolated proteins with higher frequency than in the whole Arabidopsis proteome.