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Induction of secondary dormancy by hypoxia in barley grains and its hormonal regulation.

ABSTRACT: In barley, primary dormant grains did not germinate at 30 °C in air and at 15 °C in an atmosphere containing less than 10% O2, while they germinated easily at 15 °C in air. O2 tension in embryos measured with microsensors was 15.8% at 15 °C but only 0.3% at 30 °C. Incubation of grains at 30 °C is known to induce secondary dormancy in barley, and it was shown here that secondary dormancy was also induced by a 3 d treatment in O2 tensions lower than 10% at 15 °C. After such treatments, the grains lost their ability to germinate subsequently at 15 °C in air. During seed treatment in 5% O2, embryo abscisic acid (ABA) content decreased more slowly than in air and was not altered after transfer into air. Hypoxia did not alter the expression of ABA metabolism genes after 1 d, and induction of HvNCED2 occurred only after 3 d in hypoxia. Embryo sensitivity to ABA was similar in both primary and hypoxia-induced secondary dormant grains. Gibberellic acid (GA) metabolism genes were highly regulated and regulated earlier by the hypoxia treatment, with major changes in HvGA2ox3, HvGA3ox2 and HvGA20ox1 expression after 1 d, resulting in reduced GA signalling. Although a high temperature has an indirect effect on O2 availability, the data showed that it did not affect expression of prolyl-4-hydroxylases and that induction of secondary dormancy by hypoxia at 15 °C or by high temperature in air involved separate signalling pathways. Induction by hypoxia at 15 °C appears to be more regulated by GA and less by ABA than the induction by high temperature.

SUBMITTER: Hoang HH

PROVIDER: S-EPMC3638829 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature

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Induction of secondary dormancy by hypoxia in barley grains and its hormonal regulation.

Hoang Hai Ha HH Bailly Christophe C Corbineau Françoise F Leymarie Juliette J

Journal of experimental botany 20130321 7

In barley, primary dormant grains did not germinate at 30 °C in air and at 15 °C in an atmosphere containing less than 10% O2, while they germinated easily at 15 °C in air. O2 tension in embryos measured with microsensors was 15.8% at 15 °C but only 0.3% at 30 °C. Incubation of grains at 30 °C is known to induce secondary dormancy in barley, and it was shown here that secondary dormancy was also induced by a 3 d treatment in O2 tensions lower than 10% at 15 °C. After such treatments, the grains ...[more]

PMID: 23519728

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Project description: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 accumulation 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 6 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 characterized 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.

Project description: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 accumulation 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 wasere reduced while remaining members of the same family were not affected. The N-terminal signal region was removed by proteolysis during co-translation. , evidenced by a notable absence of the predicted peptides despite near complete protein sequence coverage. In addition to a suite of previously characterised hordeins, two novel barley B-hordein isoforms and two avenin-like proteins (ALPs), 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 are due tocomprise the hordein family and the final hordein concentration affects the quality of baked and brewed products. Hordeins are members of the gluten protein family and consumption can trigger health conditions such as coeliac disease, non-coeliac gluten sensitivity, and gluten allergy. It is therefore important to study the accumulation of these proteinshordeins as this knowledge may assist plant breeding for improved health outcomes (by minimizing triggering of detrimental immune responses), nutrition and food reduced coeliac reactivity.processing properties.

Dataset Information

Induction of secondary dormancy by hypoxia in barley grains and its hormonal regulation.

Publications

Induction of secondary dormancy by hypoxia in barley grains and its hormonal regulation.

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