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Proteomics Data: Hordein accumulation in developing barley grains
Proteomics data collected as part of the manuscript by Tanner et al (2019) Frontiers in Plant Science
Abstract: The temporal pattern of accumulation of hordein storage proteins in developing barley grains was studied by enzyme-linked immunosorbent assay (ELISA), western blot and liquid chromatography tandem mass spectrometry (LC-MS/MS). Hordein acc... moreumulation was compared to the pattern seen for two abundant control proteins, serpin Z4 (an early accumulator) and lipid transferase protein (LTP1, a late accumulator). Hordeins were detected from six days post-anthesis (DPA) and peaked at 30 DPA. Changes in fresh weight indicate that desiccation begins at 20 DPA and by 37 DPA fresh weight had decreased by 35%. ELISA analysis of hordein content, expressed on a protein basis, increased to a maximum at 30 DPA followed by a 17% decrease by 37 DPA. The accumulation of 39 tryptic and 29 chymotryptic hordein peptides representing all classes of hordein was studied by LC-MS/MS. Most peptides increased to a maximum at 30 DPA, and either remained at the maximum or did not decrease significantly. Only five tryptic peptides, members of the related B1- and γ1-hordeins decreased significantly by 21-51% at 37 DPA. Thus, the concentration of some specific peptides was reduced while remaining members of the same family were not affected. The N-terminal signal region was removed by proteolysis during co-translation. In addition to a suite of previously characterised hordeins, two novel barley B-hordein isoforms mapping to wheat low molecular weight glutenins (LMW-GS-like B-hordeins), and two avenin-like proteins (ALPs) sharing homology with wheat ALPs, were identified. These identified isoforms have not previously been mapped in the barley genome. Cereal storage proteins provide significant nutritional content for human consumption and seed germination. In barley, the bulk of the storage proteins comprise the hordein family and the final hordein concentration affects the quality of baked and brewed products. It is therefore important to study the accumulation of hordeins as this knowledge may assist plant breeding for improved health outcomes (by minimizing triggering of detrimental immune responses), nutrition and food processing properties. less
Crop and Pasture Biochemistry and Physiology
Proteins and Peptides
Proteomics and Intermolecular Interactions (excl. Medical Proteomics)
multiple reaction monitoring mass spectrometry (MRM-MS)
Proteins extracted from developing barley grain, digested with either trypsin or chymotrypsin. Peptides were analysed by LC-MS on a 6500QTRAP LC-MS system. Raw data deposited in .wiff/.wiff.scan format.
Gregory J. Tanner produced the grain samples.
Malcolm J. Blundell grew and milled grain.
Michelle L. Colgrave performed sample preparation and data acquisition.
Creative Commons Attribution 4.0 International Licence
CSIRO (Australia), The University of Melbourne (Australia), La Trobe University (Australia)
Colgrave, Michelle; Tanner, Gregory; Blundell, Malcolm; Howitt, Crispin; Bacic, Antony (2019): Proteomics Data: Hordein accumulation in developing barley grains. v2. CSIRO. Data Collection.
All Rights (including copyright) CSIRO 2019.
The metadata and files (if any) are available to the public.
Livestock - Testing & Services
Mass spectrometry data collected for gluten project (Greg Tanner)