Proteomics

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Proteomic analysis of fractions of Arabidopsis thaliana proteins captured by immobilized metal affinity chromatography

ABSTRACT: Proteins from plant shoot and root tissues were extracted from wild-type Arabidopsis thaliana ecotype Columbia (Col-0). They were enriched on conditioned U(VI)-loaded and U(VI)-free Duolite C467 beads. The enriched proteins were identified and quantified by label-free shotgun proteomics.

INSTRUMENT(S): LTQ Orbitrap XL

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Root, Leaf

SUBMITTER: Jean ARMENGAUD  

LAB HEAD: Jean Armengaud

PROVIDER: PXD033354 | Pride | 2023-02-04

REPOSITORIES: Pride

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Dataset's files

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Action DRS
F102697.dat Other
F102697_p0.05.mzid.gz Mzid
F102698.dat Other
F102698_p0.05.mzid.gz Mzid
F102699.dat Other
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Publications

Uranium (U) is a naturally-occurring radionuclide that is toxic to living organisms. Given that proteins are primary targets of U(VI), their identification is an essential step towards understanding the mechanisms of radionuclide toxicity, and possibly detoxification. Here, we implemented a chromatographic strategy including immobilized metal affinity chromatography to trap protein targets of uranyl in Arabidopsis thaliana. This procedure allowed the identification of 38 uranyl-binding proteins  ...[more]

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