title: Quantitative Proteomics Analysis of Camelina sativa Seeds Overexpressing the AGG3 Gene to Identify the Proteomic Basis of Increased Yield and Stress Tolerance.
abstract: Camelina sativa, a close relative of Arabidopsis, is an oilseed plant that is emerging as an important biofuel resource. The genome and transcriptome maps of Camelina have become available recently, but its proteome composition remained unexplored. A labeling LC-based quantitative proteomics approach was applied to decipher the Camelina seed proteome, which led to the identification of 1532 proteins. In addition, the effect of overexpression of the Arabidopsis G-protein γ subunit 3 (AGG3) on the Camelina seed proteome was elucidated to identify the proteomic basis of its increased seed size and improved stress tolerance. The comparative analysis showed a significantly higher expression of proteins involved in primary and secondary metabolism, nucleic acid and protein metabolism, and abscisic acid related responses, corroborating the physiological effects of AGG3 overexpression. More importantly, the proteomic data suggested involvement of the AGG3 protein in the regulation of oxidative stress and heavy metal stress tolerance. These observations were confirmed by the physiological and biochemical characterization of AGG3-overexpressing seeds, which exhibit a higher tolerance to exogenous cadmium in a glutathione-dependent manner. The activity of multiple redox-regulating enzymes is higher in seeds expressing enhanced levels of AGG3. Overall, these data provide critical evidence for the role of redox regulation by the AGG3 protein in mediating important seed-related traits.
authors.affiliation: †Donald Danforth Plant Science Center, 975 North Warson Road, St. Louis, Missouri 63132, United States.
authors.forename: Sophie
authors.initials: S
authors.lastname: Alvarez
authors.affiliation: †Donald Danforth Plant Science Center, 975 North Warson Road, St. Louis, Missouri 63132, United States.
authors.forename: Swarup
authors.initials: S
authors.lastname: Roy Choudhury
authors.affiliation: ‡Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599, United States.
authors.forename: Kumaran
authors.initials: K
authors.lastname: Sivagnanam
authors.affiliation: ‡Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599, United States.
authors.forename: Leslie M
authors.initials: LM
authors.lastname: Hicks
authors.affiliation: †Donald Danforth Plant Science Center, 975 North Warson Road, St. Louis, Missouri 63132, United States.
authors.forename: Sona
authors.initials: S
authors.lastname: Pandey
mesh_terms: D000222:Adaptation, Physiological; D019607:Brassicaceae / Q000196:embryology / Q000378:metabolism* / Q000502:physiology; D002853:Chromatography, Liquid; D017343:Genes, Plant; D019216:Metals, Heavy / Q000633:toxicity; D018384:Oxidative Stress; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D040901:Proteomics; D012639:Seeds / Q000378:metabolism*; D013312:Stress, Physiological; D053719:Tandem Mass Spectrometry
chemical_list: D019216:Metals, Heavy; D010940:Plant Proteins
keywords: AGG3; Camelina sativa; iTRAQ; quantitative proteomics; redox regulation; seed proteome