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 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). Analysis of CCB-stained gels (PDQuest) reproducibly detected 214 spots, and 64 proteins differentially expressed were identified using LC-MS/MS. In both populations, Cu excess impacted both light-dependent (OEE, cytochrome b6-f complex, and chlorophyll a-b binding protein), and -independent (RuBisCO) photosynthesis reactions, more intensively in NM leaves (ferredoxin-NADP reductase and metalloprotease FTSH2). In both populations, upregulation of isocitrate dehydrogenase and cysteine/methionine synthases respectively suggested increased isocitrate oxidation and enhanced need for S-containing amino-acids, likely for chelation and detoxification. In NM leaves, an increasing need for energetic compounds was indicated by the stimulation of ATPases, glycolysis, pentose phosphate pathway, and Calvin cycle enzymes; impacts on protein metabolism and oxidative stress increase were respectively suggested by the rise of chaperones and redox enzymes. Overexpression of a HSP70 may be pivotal for M Cu tolerance by protecting protein metabolism. All MS data have been deposited in the ProteomeXchange with the dataset identifier PXD001930 (http//proteomecentral.proteomexchange.org/dataset/PXD001930).

Influence of Heavy Metals (Ni, Cu, and Zn) on Nitro-Oxidative Stress Responses, Proteome Regulation and Allergen Production in Basil (Ocimum basilicum L.) Plants

“…Ribosomal protein L14 is one of many proteins that form a large ribosomal subunit (60S) and is considered to play a main role in the ribonucleoprotein complex ( Davies et al, 1996 ), while ribulose-1,5-bisphosphate carboxylase/oxygenase (also known as RuBisCO) is a key enzyme involved in the first step of carbon assimilation during the Calvin cycle ( Spreitzer and Salvucci, 2002 ). This observed upregulation comes in agreement with several proteomic analyses of plants under Cu contamination, which identified similar protein components to be induced ( Ahsan et al, 2007 ; Hego et al, 2016 ; Wang et al, 2017 ), likely in an attempt by the plants to fuel defense mechanisms in response to stress imposition via increased primary metabolism pathways.…”

RETRACTED: Morpho-Physiological and Proteomic Analyses of Eucalyptus camaldulensis as a Bioremediator in Copper-Polluted Soil in Saudi Arabia

“…Their findings revealed variations in the protein expression pattern for reinstating cellular homeostasis, where two proteins were suppressed, seven proteins were down regulated, and five proteins were up regulated. Some proteomic studies were focused on Cu stress in Arabidopsis thaliana [24], Cannabis sativa roots L. [23], Oryza sativa [25], and Agrostis capillaris [26].…”

Post‐transcriptional adaptation of the aquatic plant Spirodela polyrhiza under stress and hormonal stimuli

“…This change in post‐transcriptional regulation is of importance when extrapolating laboratory results to duckweed growing outdoors because most laboratories use sucrose in their growth media. Copper stress caused the cleavage of mRNAs encoding two polyphenol oxidases, reminiscent of the decrease in protein levels observed with non‐tolerant Agrostis capilaris (Hego et al ., ). The mRNA encoding respiratory burst oxidase homolog protein E was also cleaved, demonstrating a strong enrichment for ROS regulation under this growth condition.…”