The legumin-like storage protein of Lupinus albus seeds

Duranti, Marcello; Guerrieri, N.; Takahashi, Tsuyoshi; Cerletti, Paolo

doi:10.1016/0031-9422(88)80586-7

Cited by 41 publications

(45 citation statements)

References 22 publications

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“…Glycosylations could cause this molecular mass difference. Glycosylations are normally not found in legumins; however, glycosylated legumins are found in lupin (Lupinus albus) and Japanese red cedar (Cryptomeria japonica; Duranti et al, 1988;Wind and Häger, 1996). The common N-glycosylation motif, Asn-X-Ser/Thr, is lacking in LLP2 and LLP3.…”

Section: Globulin Seed Storage Proteins and Globulin Genes In Lotusmentioning

confidence: 99%

The Proteome of Seed Development in the Model Legume Lotus japonicus

et al. 2009

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We have characterized the development of seeds in the model legume Lotus japonicus. Like soybean (Glycine max) and pea (Pisum sativum), Lotus develops straight seed pods and each pod contains approximately 20 seeds that reach maturity within 40 days. Histological sections show the characteristic three developmental phases of legume seeds and the presence of embryo, endosperm, and seed coat in desiccated seeds. Furthermore, protein, oil, starch, phytic acid, and ash contents were determined, and this indicates that the composition of mature Lotus seed is more similar to soybean than to pea. In a first attempt to determine the seed proteome, both a two-dimensional polyacrylamide gel electrophoresis approach and a gel-based liquid chromatography-mass spectrometry approach were used. Globulins were analyzed by two-dimensional polyacrylamide gel electrophoresis, and five legumins, LLP1 to LLP5, and two convicilins, LCP1 and LCP2, were identified by matrix-assisted laser desorption ionization quadrupole/time-of-flight mass spectrometry. For two distinct developmental phases, seed filling and desiccation, a gel-based liquid chromatography-mass spectrometry approach was used, and 665 and 181 unique proteins corresponding to gene accession numbers were identified for the two phases, respectively. All of the proteome data, including the experimental data and mass spectrometry spectra peaks, were collected in a database that is available to the scientific community via a Web interface (http://www.cbs.dtu.dk/cgi-bin/lotus/db.cgi). This database establishes the basis for relating physiology, biochemistry, and regulation of seed development in Lotus. Together with a new Web interface (http:// bioinfoserver.rsbs.anu.edu.au/utils/PathExpress4legumes/) collecting all protein identifications for Lotus, Medicago, and soybean seed proteomes, this database is a valuable resource for comparative seed proteomics and pathway analysis within and beyond the legume family.

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Section: Globulin Seed Storage Proteins and Globulin Genes In Lotusmentioning

confidence: 99%

The Proteome of Seed Development in the Model Legume Lotus japonicus

et al. 2009

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“…In Arabidopsis thaliana (thale cress) and other crucifers, the main seed proteins are the 12 S globulins (cruciferin) and the 2 S albumins (napin), which are localized to PSVs (protein storage vacuoles), and the oleosins, which are integral proteins of the oil-body membrane. Salt-soluble globulins are widely distributed in dicotyledons, monocotyledons and gymnosperms, and comprise the trimeric and predominantly glycosylated 7 S vicilins and the hexameric and generally non-glycosylated 11-12 S legumins [1]. The three-dimensional structures of several vicilin-type proteins, namely phaseolin [2], canavalin [3], β-conglycinin [4] and germin [5], and the legumin-type proglycinin A1aB1b homotrimer [6] and glycinin A3B4 homohexamer [7], have revealed that seed storage globulins share striking similarities in secondary and tertiary structure with the cupin superfamily of prokaryotic and eukaryotic proteins [8,9].…”

Section: Introductionmentioning

confidence: 99%

“…1 To whom correspondence should be addressed (email andrew.ross@nrc-cnrc.gc.ca). molecular activation/de-activation of signal-transduction pathways.…”

Section: Introductionmentioning

confidence: 99%

Phosphorylation of the 12 S globulin cruciferin in wild-type and abi1-1 mutant Arabidopsis thaliana (thale cress) seeds

Wan

Ross

Yang

et al. 2007

Biochemical Journal

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Cruciferin (a 12 S globulin) is the most abundant storage protein in the seeds of Arabidopsis thaliana (thale cress) and other crucifers, sharing structural similarity with the cupin superfamily of proteins. Cruciferin is synthesized as a precursor in the rough endoplasmic reticulum. Subunit assembly is accompanied by structural rearrangements involving proteolysis and disulfidebond formation prior to deposition in protein storage vacuoles. The A. thaliana cv. Columbia genome contains four cruciferin loci, two of which, on the basis of cDNA analysis, give rise to three alternatively spliced variants. Using MS, we confirmed the presence of four variants encoded by genes At4g28520.1, At5g44120.3, At1g03880.1 and At1g3890.1 in A. thaliana seeds. Two-dimensional gel electrophoresis, along with immunological detection using anti-cruciferin antiserum and antibodies against phosphorylated amino acid residues, revealed that cruciferin was the major phosphorylated protein in Arabidopsis seeds and that polymorphism far exceeded that predicted on the basis of known isoforms. The latter may be attributed, at least in part, to phosphorylation site heterogeneity. A total of 20 phosphorylation sites, comprising nine serine, eight threonine and three tyrosine residues, were identified by MS. Most of these are located on the IE (interchain disulfide-containing) face of the globulin trimer, which is involved in hexamer formation. The implications of these findings for cruciferin processing, assembly and mobilization are discussed. In addition, the protein phosphatase 2C-impaired mutant, abi1-1, was found to exhibit increased levels of cruciferin phosphorylation, suggesting either that cruciferin may be an in vivo target for this enzyme or that abi1-1 regulates the protein kinase/phosphatase system required for cruciferin phosphorylation.

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“…Under the conditions considered in the present paper, the equilibrium between the legumin oligomers in mature lupin seeds is biased toward the hexamer [5,7]. A modified 7s component lacking the M , 52000 polypeptide is also present, and does not assemble to a 12s form [5].While the majority of legumin-like polypeptides have no bound sugar, lupin legumin-like protein, which will be referred to as legumin, is anomalous in being glycosylated [5].In lupin, the protease which processes the legumin precursor polypeptides appears approximately ten days after synthesis has begun, and this allows a transient accumulation of propolypeptides [6, 81. In other seeds, the legumin precursor is processed within a few hours of synthesis [9].…”

mentioning

confidence: 95%

“…In the legumin-like protein of mature Lupinus albus the subunits contain CI polypeptides with M , 47000-52000 or 42 000 -44000 and fl polypeptides of M , 20 000 -22 000 [5].…”

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confidence: 99%

The legumin precursor from white lupin seed

Duranti

Guerrieri

Cerletti

et al. 1992

European Journal of Biochemistry

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The precursors of the legumin-like storage protein from developing white lupin seeds (35 days after flowering) are trimers composed of protomers of M , 72000 or 67000. Some subunits of these oligomers contain processed precursor polypeptides, namely a polypeptides of either 52 000 or 44000 linked through disulphide bonds to a fl polypeptide of 21 000, typical of the mature legumin. The prolegumin is glycosylated.Legumin oligomers purified from the same seeds are both trimers and hexamers; some of their subunits are still made of precursor polypeptides. The hexamer contains less precursor polypeptide than the trimer. A low level or absence of precursor appears to be a condition of hexamer assembly. The heterogenous prolegumin and legumin oligomers represent intermediates in the processing of the prolegumin to mature legumin.Hydrophobic-interaction chromatography on TSK-phenyl-SPW and titration with the hydrophobic probe 8-anilino-1-naphthalenesulphonate indicate that the legumin is less hydrophobic than the prolegumin. This is attributed to structural rearrangements at processing of the propolypeptide, made evident by the behaviour in CD and by the second-derivative ultraviolet spectra of the two proteins.The total protein extract of developing cotyledons at 40 days after flowering contains endopeptidases, similar to those existing in the resting seeds, which cause a limited cascade degradation of the prolegumin and legumin.The subunits of legumin-like protein oligomers of monocotyledonous and dicotyledonous seeds are synthesized as prepropolypeptides. Cotranslational proteolytic removal of the signal peptide produces propolypeptides, which assemble in the endoplasmic reticulum to form trimers, with sedimentation coefficient 7 -SS, and are transferred to protein bodies.Within the protein bodies, the propolypeptides are cleaved into (x and fl polypeptides, also named the acidic and basic polypeptides, respectively, linked through a disulphide bridge(s), which form the mature legumin subunit. The disulphide linkage exists in the propolypeptide prior to cleavage. All these events are reviewed in [l, 21. The 12s hexamers of legumin-like proteins are formed only after processing of the prolegumin to mature legumin [3, 41. In vitro study of glycinin from the soybean have shown that while there is sufficient flexibility in the hexameric form to accomodate a small proportion of proglycinin monomers, trimers of proglycinin will not associate, either mutually or with the trimers of mature glycinin subunits, to give rise to hexamers [4].In the legumin-like protein of mature Lupinus albus the subunits contain CI polypeptides with M , 47000-52000 or These homologous but heterogenous subunits [6] are presumably encoded by a multigene family, as is the case for the legumin-like proteins of other seeds [2]. In lupin the 12s oligomers are in equilibrium with a 7s form [5]; hexameric and trimeric structures, respectively, have been proposed for them [S], analogous to other legumin-like proteins. Under the conditions considered ...

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The legumin-like storage protein of Lupinus albus seeds

Cited by 41 publications

References 22 publications

The Proteome of Seed Development in the Model Legume Lotus japonicus

The Proteome of Seed Development in the Model Legume Lotus japonicus

Phosphorylation of the 12 S globulin cruciferin in wild-type and abi1-1 mutant Arabidopsis thaliana (thale cress) seeds

The legumin precursor from white lupin seed

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