Proteomics

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Copper stress-induced changes in leaf soluble proteome of Cu-sensitive and tolerant Agrostis capillaris L. populations


ABSTRACT: Changes in leaf soluble proteome were explored in 3-month-old plants of Cu-tolerant (metallicolous, M) and sensitive (non-metallicolous, NM) Agrostis capillaris L. populations exposed to increasing Cu concentrations (1-50 µM). Aims of the study were to investigate (1) differential protein expression in NM and M leaves under increasing Cu exposure, and (2) molecular mechanisms underlying higher Cu tolerance in M plants. Plants were cultivated on perlite (CuSO4 spiked-nutrient solution); fresh leaf aliquots were frozen in liquid nitrogen. Soluble leaf proteins were extracted by the trichloroacetic acid/acetone procedure, and separated with 2-DE (linear 4-7 pH gradient). Analysis of CCB-stained gels (PDQuest) reproducibly detected 214 spots, of which 107 were analyzed using LC-MS/MS.

INSTRUMENT(S): LCQ Deca XP Plus

ORGANISM(S): Agrostis Capillaris (colonial Bentgrass) (agrostis Tenuis)

TISSUE(S): Leaf

SUBMITTER: Stephane Claverol  

LAB HEAD: Marc Bonneu

PROVIDER: PXD001930 | Pride | 2016-04-12

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
eh130924_1101.RAW Raw
eh130924_1101_Agrostis.msf Msf
eh130924_1101_Viridiplantae.msf Msf
eh130924_1104.RAW Raw
eh130924_1104_Agrostis.msf Msf
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Publications

Copper stress-induced changes in leaf soluble proteome of Cu-sensitive and tolerant Agrostis capillaris L. populations.

Hego Elena E   Vilain Sébastien S   Barré Aurélien A   Claverol Stéphane S   Dupuy Jean-William JW   Lalanne Céline C   Bonneu Marc M   Plomion Christophe C   Mench Michel M  

Proteomics 20160501 9


Changes in leaf soluble proteome were explored in 3-month-old plants of metallicolous (M) and nonmetallicolous (NM) Agrostis capillaris L. populations exposed to increasing Cu concentrations (1-50 μM) to investigate molecular mechanisms underlying plant responses to Cu excess and tolerance of M plants. Plants were cultivated on perlite (CuSO4 spiked-nutrient solution). Soluble proteins, extracted by the trichloroacetic acid/acetone procedure, were separated with 2-DE (linear 4-7 pH gradient). An  ...[more]

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