Distribution of Napin and Cruciferin in Developing Rape Seed Embryos

Höglund, Anders; Rödin, Joakim; Larsson, Erik; Rask, Lars

doi:10.1104/pp.98.2.509

Cited by 95 publications

(56 citation statements)

References 20 publications

(27 reference statements)

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“…This low molecular weight fraction was the second most abundant one in ASP reaching 21.7% of total proteins. The 20-and 33 kDa fractions, also found in both protein products, correspond to α-and β-subunits of cruciferin as described by Höglund et al (1992). The 53kDa fraction, also observed by Aluco and McIntosh (2001), was present only in PI but not in ASP (Fig.…”

Section: Protein Profile Of Pi and Aspsupporting

confidence: 77%

Comparative biochemical profile of protein-rich products obtained from industrial rapeseed meal

Ivanova

Kalaydzhiev

Rustad

et al. 2017

Emir. J. Food Agric

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Section: Protein Profile Of Pi and Aspsupporting

confidence: 77%

Comparative biochemical profile of protein-rich products obtained from industrial rapeseed meal

Ivanova

Kalaydzhiev

Rustad

et al. 2017

Emir. J. Food Agric

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“…This difference in the expression pattern between At2S3 and CRC is consistent with the study in developing rape seed embryos (Brassica napus) whereby the synthesis of napin started a few days earlier than that of cruciferin. 9 To further corroborate the finding that accumulation of seed storage proteins is influenced by disruption of the ASIL1 gene, we compared the 12S CRC accumulation profiles in asil1-1 and wild-type plants by immunoblot analysis. Proteins were extracted Figure 1.…”

Section: Asil1 Is Required For Proper Timing Of Seed Filling In Arabimentioning

confidence: 99%

ASIL1 is required for proper timing of seed filling in Arabidopsis

Gao

Lui

et al. 2011

Plant Signaling & Behavior

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Seeds offer plants a unique opportunity to suspend their life cycles in a desiccated state. This enables them to endure adverse environmental conditions and then resume growth using endogenous storage reserves when more favorable conditions develop. Seed formation is an intricate genetically programmed process that is correlated with changes in metabolite levels and is regulated by a complex signaling network mediated mainly by hormone and sugar levels. 3,4 Seed development can be divided into two stages, embryo morphogenesis and maturation. The hallmarks of maturation include storage compound accumulation, acquisition of desiccation tolerance, growth arrest and entry into a dormancy period that is broken upon germination. 5 In Arabidopsis, three members of the B3 family of transcription factors, LEAFY COTYLEDON (LEC) 2, ABSCISIC ACID-INSENTITIVE 3 (ABI3) and FUSCA 3 (FUS3) as well as a fourth regulator, a HAP3 subunit of the CCAAT-box binding transcription factor (CBF) LEC1, are master regulators of seed maturation processes. A redundant gene regulatory network linking these regulators was elucidated by examining the expression of ABI3, FUS3 and LEC2 in abi3, fus3, lec1 and lec2 single, double and triple mutants. 6 In combination with ABA, GA, auxin and sugar signaling, this regulatory network governs most seed-specific maturation traits in a partially redundant manner. 6 The regulatory networks controlling the seed maturation program in flowering plants are repressed prior to germination so that seed storage reserves do not accumulate during vegetativeIn flowering plants, seed development and seed filling are intricate genetically programmed processes that correlate with changes in metabolite levels and that are spatially and temporally regulated by a complex signaling network mediated mainly by sugars and hormones. ASIL1, a member of the plant-specific trihelix family of DNA-binding transcription factors, was isolated based on its interaction with the GT-element of the Arabidopsis thaliana 2S albumin At2S3 promoter. Mutation of ASIL1 derepressed expression of a subset of embryonic genes resulting in accumulation of 2S albumin and embryo-specific lipids in leaves. 1 It was recently reported that mutation of ASIL1 led to early embryo development in Arabidopsis. 2 In this study, we demonstrated that ASIL1 acts as a temporal regulator of seed filling. In developing siliques, mutation of ASIL1 led to earlier expression of master regulatory genes LEC2, FUS3 and ABI3 as well as genes for seed storage reserves. Moreover, the 12S globulin accumulated to a much higher level in the developing seeds of asil1-1 compared to wild type. To our knowledge, this is the first evidence that ASIL1 not only functions as a negative regulator of embryonic traits in seedlings but also contributes to the maintenance of precise temporal control of seed filling. Thus, ASIL1 represents a novel component of the regulatory framework controlling embryonic gene expression in Arabidopsis.

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“…Mobilization of stored compounds in germinating seeds does not occur in all cells and tissues simultaneously but follows specific spatial and temporal patterns (Hara and Matsubara, 1980;Bethke et al, 1998;Tiedemann et al, 2000). These changes have been documented by following globulin mobilization using both histological stains and immunohistochemical analyses (Hö glund et al, 1992;Tiedemann et al, 2000). For example, in vetch (Vicia sativa), the first storage proteins to be mobilized, 2 to 3 d post germination, are those located in embryo axis cells; mobilization of the globulins stored in the cotyledons typically starts thereafter (Schlereth et al, 2000;Tiedemann et al, 2000).…”

mentioning

confidence: 99%

Protein Storage Vacuoles Are Transformed into Lytic Vacuoles in Root Meristematic Cells of Germinating Seedlings by Multiple, Cell Type-Specific Mechanisms

Zheng

Staehelin

2011

Plant Physiology

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We have investigated the structural events associated with vacuole biogenesis in root tip cells of tobacco (Nicotiana tabacum) seedlings preserved by high-pressure freezing and freeze-substitution techniques. Our micrographs demonstrate that the lytic vacuoles (LVs) of root tip cells are derived from protein storage vacuoles (PSVs) by cell type-specific sets of transformation events. Analysis of the vacuole transformation pathways has been aided by the phytin-dependent black osmium staining of PSV luminal contents. In epidermal and outer cortex cells, the central LVs are formed by a process involving PSV fusion, storage protein degradation, and the gradual replacement of the PSV marker protein a-tonoplast intrinsic protein (TIP) with the LV marker protein g-TIP. In contrast, in the inner cortex and vascular cylinder cells, the transformation events are more complex. During mobilization of the stored molecules, the PSV membranes collapse osmotically upon themselves, thereby squeezing the vacuolar contents into the remaining bulging vacuolar regions. The collapsed PSV membranes then differentiate into two domains: (1) vacuole "reinflation" domains that produce pre-LVs, and (2) multilamellar autophagosomal domains that are later engulfed by the pre-LVs. The multilamellar autophagosomal domains appear to originate from concentric sheets of PSV membranes that create compartments within which the cytoplasm begins to break down. Engulfment of the multilamellar autophagic vacuoles by the pre-LVs gives rise to the mature LVs. During pre-LV formation, the PSV marker a-TIP disappears and is replaced by the LV marker g-TIP. These findings demonstrate that the central LVs of root cells arise from PSVs via cell type-specific transformation pathways.

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Distribution of Napin and Cruciferin in Developing Rape Seed Embryos

Cited by 95 publications

References 20 publications

Comparative biochemical profile of protein-rich products obtained from industrial rapeseed meal

Comparative biochemical profile of protein-rich products obtained from industrial rapeseed meal

ASIL1 is required for proper timing of seed filling in Arabidopsis

Protein Storage Vacuoles Are Transformed into Lytic Vacuoles in Root Meristematic Cells of Germinating Seedlings by Multiple, Cell Type-Specific Mechanisms

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