Analysis of in vivo and in vitro Globulin Formation during Cotyledon Development of Field Beans (V icia faba L. var. minor)

Bassüner, Ronald; Manteuffel, Renate; Müntz, Klaus; Püchel, Manfred; Schmidt, P; Weber, Ernst

doi:10.1016/s0015-3796(83)80081-x

Cited by 27 publications

(10 citation statements)

References 48 publications

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“…Since in Vicia faba cotyledons the USP gene expression decreases whereas the legumin B4 gene expression increases around the middle of seed development [2] we speculate that at this developmental stage the RY motif and its postulated binding factor might be involved both in the down-regulation of a set of genes represented by the USP gene and the up-regulation of another set of genes represented by the legumin B4 gene.…”

Section: The Basic Promoter Governs the Seed Specificity Of Usp Exprementioning

confidence: 90%

“…minor, an usp message appears before day 29 of seed development, reaches a maximum during the midst of the developmental time course and declines to low values in mature seeds [2]. To investigate the temporal expression pattern of the described gus deletion constructs we chose three to six plants of each transgenic line exhibiting GUS activity in mature seeds near the mean value of all available plants carrying that construct.…”

Section: Several Promoter Elements Exert Temporal Control Of Usp Exprmentioning

confidence: 99%

“…minor cv. Fribo [2]. The 30 kDa USP protein most likely exists as dimer and turns over rapidly; its function is unknown [31. We chose the USP gene promoter because (1) it is predominantly seed-specific like the legumin B4 promoter studied previously [7], (2) it is 5 to 10 times stronger in driving reporter genes [27]; (3) its activity peak is shifted towards earlier developmental stages in comparison to the legumin B4 gene promoter [2]; (4) it contains several sequence motifs found in seed storage protein gene promoters (see Results) but (5) it is expected to be different from the more intensively studied promoters of the legumin and vicilin type (for review see [32]) due to the different nature and (unknown) function of the protein encoded by the USP gene(s).…”

Section: Introductionmentioning

confidence: 99%

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A complex ensemble of cis-regulatory elements controls the expression of a Vicia faba non-storage seed protein gene

et al. 1993

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We have identified cis-regulatory elements within the 5'-upstream region of a Vicia faba non-storage seed protein gene, called usp, by studying the expression of usp-promoter deletion fragments fused to reporter genes in transgenic tobacco seeds. 0.4 kb of usp upstream sequence contain at least six, but probably more, distinct cis-regulatory elements which are responsible for seemingly all quantitative, spatial and temporal aspects of expression. Expression-increasing and -decreasing elements are interspersed and include an AT-rich sequence, a G-box element and a CATGCATG motif. The latter acts as a negative element in contrast to what has been found for the same motif in legumin- and vicilin-type seed storage protein gene promoters. Seed specificity of expression is mainly determined by the -68/+51 region which confers, however, only very low levels of expression. The data support the combinatorial model of promoter function.

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Section: The Basic Promoter Governs the Seed Specificity Of Usp Exprementioning

confidence: 90%

Section: Several Promoter Elements Exert Temporal Control Of Usp Exprmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A complex ensemble of cis-regulatory elements controls the expression of a Vicia faba non-storage seed protein gene

et al. 1993

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“…This expectation was experimentally con®rmed. The size of the legumin precursor corresponded to prolegumin B which has a MW of 52 kDa (cDNA-derived according to BaÈ umlein et al 1986) but always occupies a position with the relative MW of 62 kDa on SDS polyacrylamide gels (BassuÈ ner et al 1983b). When proteinase K was added posttranslationally to the incubation mixture the legumin B precursor that had been translated from ASP-mRNA disappeared whereas that translated from +SP-mRNA remained intact (Fig.…”

Section: Resultsmentioning

confidence: 99%

Subcellular localization of the 2S globulin narbonin in seeds of Vicia narbonensis

Steffens¹,

Hải²,

Hillmer³

et al. 1997

Planta

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Narbonin is a 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) cotyledons. Its amino acid composition and the pattern of its regulated accumulation in developing seeds led to the suggestion that narbonin could be a storage protein. Therefore, it was expected to be present in protein bodies of the storage tissue cells. Comparison of the cDNA-derived amino acid sequence with a directly determined partial N-terminal sequence revealed that the primary translation product of narbonin mRNA lacks a transient N-terminal signal peptide (V.H. Nong et al., 1995, Plant Mol Biol 28: 61 - 72). Narbonin polypeptides that had been synthesized in a cell-free translation system supplemented with dog pancreas microsomes were not protected against degradation by posttranslationally added proteases (protease protection assay). In accordance with the lack of a signal peptide this indicates that the polypeptide was not cotranslationally sequestered into the microsomes. The protein-body fraction that had been isolated from mature narbon bean cotyledons by a non-aqueous gradient centrifugation procedure was free of narbonin; this was found in the soluble cell fraction. In electron micrographs, narbonin could be localized in the cytoplasm using the immuno gold-labelling technique. Previously, it had already been shown that narbonin is too slowly degraded during narbon bean germination to act as a storage protein. From all these results it has to be concluded that narbonin is a cytoplasmic protein which does not belong to the storage proteins in the restricted sense. Other possible functions are discussed.

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“…The size of the legumin precursor corresponded to prolegumin B which has a MW of 52 kDa (cDNA-derived according to BaÈ umlein et al 1986) but always occupies a position with the relative MW of 62 kDa on SDS polyacrylamide gels (BassuÈ ner et al 1983b). This expectation was experimentally con®rmed.…”

Section: Resultsmentioning

confidence: 99%

Subcellular localization of the 2S globulin narbonin in seeds of Vicia narbonensis

Steffens

Hải

Hillmer

et al. 1997

Planta

Self Cite

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Narbonin is a 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) cotyledons. Its amino acid composition and the pattern of its regulated accumulation in developing seeds led to the suggestion that narbonin could be a storage protein. Therefore, it was expected to be present in protein bodies of the storage tissue cells. Comparison of the cDNA-derived amino acid sequence with a directly determined partial N-terminal sequence revealed that the primary translation product of narbonin mRNA lacks a transient N-terminal signal peptide (V.H. Nong et al., 1995, Plant Mol Biol 28: 61±72). Narbonin polypeptides that had been synthesized in a cell-free translation system supplemented with dog pancreas microsomes were not protected against degradation by posttranslationally added proteases (protease protection assay). In accordance with the lack of a signal peptide this indicates that the polypeptide was not cotranslationally sequestered into the microsomes. The proteinbody fraction that had been isolated from mature narbon bean cotyledons by a non-aqueous gradient centrifugation procedure was free of narbonin; this was found in the soluble cell fraction. In electron micrographs, narbonin could be localized in the cytoplasm using the immuno gold-labelling technique. Previously, it had already been shown that narbonin is too slowly degraded during narbon bean germination to act as a storage protein. From all these results it has to be concluded that narbonin is a cytoplasmic protein which does not belong to the storage proteins in the restricted sense. Other possible functions are discussed.

show abstract

Analysis of in vivo and in vitro Globulin Formation during Cotyledon Development of Field Beans (V icia faba L. var. minor)

Cited by 27 publications

References 48 publications

A complex ensemble of cis-regulatory elements controls the expression of a Vicia faba non-storage seed protein gene

A complex ensemble of cis-regulatory elements controls the expression of a Vicia faba non-storage seed protein gene

Subcellular localization of the 2S globulin narbonin in seeds of Vicia narbonensis

Subcellular localization of the 2S globulin narbonin in seeds of Vicia narbonensis

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