title: iTRAQ-based analysis of changes in the cassava root proteome reveals pathways associated with post-harvest physiological deterioration.
abstract: The short storage life of harvested cassava roots is an important constraint that limits the full potential of cassava as a commercial food crop in developing countries. We investigated the molecular changes during physiological deterioration of cassava root after harvesting using isobaric tags for relative and absolute quantification (iTRAQ) of proteins in soluble and non-soluble fractions prepared during a 96 h post-harvest time course. Combining bioinformatic approaches to reduce information redundancy for unsequenced or partially sequenced plant species, we established a comprehensive proteome map of the cassava root and identified quantitatively regulated proteins. Up-regulation of several key proteins confirmed that physiological deterioration of cassava root after harvesting is an active process, with 67 and 170 proteins, respectively, being up-regulated early and later after harvesting. This included regulated proteins that had not previously been associated with physiological deterioration after harvesting, such as linamarase, glutamic acid-rich protein, hydroxycinnamoyl transferase, glycine-rich RNA binding protein, β-1,3-glucanase, pectin methylesterase, maturase K, dehydroascorbate reductase, allene oxide cyclase, and proteins involved in signal pathways. To confirm the regulation of these proteins, activity assays were performed for selected enzymes. Together, our results show that physiological deterioration after harvesting is a highly regulated complex process involving proteins that are potential candidates for biotechnology approaches to reduce such deterioration.
authors: Department of Biology, Plant Biotechnology, Eidgenössische Technische Hochschule (ETH) Zurich, Universitätstraβe 2, 8092 Zurich, Switzerland.
authors: Judith
authors: J
authors: Owiti
authors: Jonas
authors: J
authors: Grossmann
authors: Peter
authors: P
authors: Gehrig
authors: Christophe
authors: C
authors: Dessimoz
authors: Christophe
authors: C
authors: Laloi
authors: Maria Benn
authors: MB
authors: Hansen
authors: Wilhelm
authors: W
authors: Gruissem
authors: Hervé
authors: H
authors: Vanderschuren
mesh_terms: D060387:Ascorbate Peroxidases / Q000378:metabolism; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism; D002473:Cell Wall / Q000378:metabolism; D018556:Crops, Agricultural; D030562:Databases, Protein; D015536:Down-Regulation / Q000502:physiology; D018506:Gene Expression Regulation, Plant / Q000502:physiology; D043326:Glucan 1,3-beta-Glucosidase / Q000378:metabolism; D002365:Manihot / Q000201:enzymology / Q000378:metabolism* / Q000502:physiology; D057865:Plant Immunity / Q000502:physiology; D010940:Plant Proteins / Q000145:classification / Q000378:metabolism*; D018517:Plant Roots / Q000378:metabolism*; D020543:Proteome / Q000378:metabolism; D040901:Proteomics / Q000379:methods*; D017382:Reactive Oxygen Species / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods; D013482:Superoxide Dismutase / Q000378:metabolism; D015854:Up-Regulation / Q000502:physiology
chemical_list: D010940:Plant Proteins; D020543:Proteome; D017382:Reactive Oxygen Species; D060387:Ascorbate Peroxidases; D013482:Superoxide Dismutase; D002265:Carboxylic Ester Hydrolases; C022323:pectinesterase; D043326:Glucan 1,3-beta-Glucosidase