Relationships among low MW hydrophobic proteins from wheat endosperm

Salcedo, Gabriel; Rodríguez-Loperena, M.A.; Aragoncillo, Cipriano

doi:10.1016/s0031-9422(00)94627-2

Cited by 20 publications

(14 citation statements)

References 11 publications

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“…B-D Two-dimensional gels corresponding to addition lines 1, 3, and 4, respectively been previously reported by other workers (Dolí and Brown 1979;Shewry et al 1979). The low genetic variability of CM-proteins in barley is in agreement with that observed for the same proteins in wheat, where no variants were found in an extensive survey of Triticum aestivum and T. turgidum samples, with the exception of variant CM3' of protein CM3, which was found in only two closely related T. turgidum cultivars (García-Olmedo and Garcia-Faure 1969;RodriguezLoperena et al 1975;Salcedo et al 1978). The fact that CMe-2,2' are present in 7 out of 8 H. spontaneum samples and in 11 out of 12 H. vulgare samples from Morocco indicates either intense introgression or even a possible domestication event in that área.…”

Section: Discussionsupporting

confidence: 83%

Genetics of CM-proteins (A-hordeins) in barley

Salcedo¹,

Fra-Mon²,

Molina-Cano³

et al. 1984

Theoret. Appl. Genetics

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Section: Discussionsupporting

confidence: 83%

Genetics of CM-proteins (A-hordeins) in barley

Salcedo¹,

Fra-Mon²,

Molina-Cano³

et al. 1984

Theoret. Appl. Genetics

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“…3 A and D) that corresponded to previously described CM proteins (hydrophobic endosperm globulins; refs. [25][26][27][28][29] as demonstrated by coelectrophoresis with purified components (data not shown). T. turgidum (AABB) presented CM proteins 2, 3, and 16 ( Fig.…”

Section: Resultsmentioning

confidence: 79%

Wheat tetrameric inhibitors of insect α-amylases: Alloploid heterosis at the molecular level

Gómez

Sánchez‐Monge

Garcı́a-Olmedo

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

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Tetrameric inhibitors of heterologous aamylases have been characterized in allohexaploid wheat, Triticum aestivum (genomes AABBDD), as well as in Triicum turgidum (AABB) and Triticum tauschii (DD). Their subunits have been identified as the previously described CM proteins. Single oligomeric species were observed in T. Turgidum (subunits CM2, CM3A, and CM16) and in T. tauschii (CM1, CM3D, and CM17) by a two-dimensional electrophoretic method that does not dissociate the inhibitors in the first dimension. Multiple tetrameric species, resulting from different combinations of the subunits contributed by the two ancestral species, are observed by the same procedure in T. aestivum. The three types of subunits were required for significant activity when the inhibitor of T. turgidum was reconstituted from the purified subunits, whereas, in the case of T. tauschii, binary mixtures involving subunit CM1 also had some activity. Additional combinations of the subunits present in these two species, which occur in the allohexaploid T. aestivum, were also reconstituted, and their inhibitory activities ranged from 144% to 33% the activity of the reconstituted inhibitor from T. tauschii. The activity of these inhibitors toward the a-amylase (1,4-a-D-glucan glucanohydrolase, EC 3.2.1.1) of the insect Tenebrio molitor is much greater than that against the salivary enzyme. These observations, together with the previously established chromosomal locations of genes encoding CM proteins, fit a model of alloploid heterosis at the molecular level.Allopolyploidy has played a major role in the evolution of higher plants, as possibly over one-third of the present species, including many important crops, have an obvious alloploid origin (1). At least two features inherent to an alloploid genetic structure can be considered as relevant to its apparent success: the long-term diversification or loss (diploidization) of redundant genetic information and the immediate fixation of possible intergenomic heterotic interactions. Diploidization, which can be envisaged as a mechanism of elimination of deleterious interactions, has been extensively studied in fish (refs. 2 and 3) and, to a lesser extent, in plants (4-9), but evidence of alloploid heterosis at the molecular level is lacking.Plant proteins that inhibit heterologous proteinases and a-amylases are receiving considerable attention because of recent evidence concerning their possible role in plant protection and the possibility of interspecies genetic transfer by recombinant DNA techniques (10). Subunits of tetrameric inhibitors of heterologous a-amylases are encoded in wheat and barley by multigene families that also include genes for dimeric and monomeric inhibitors of a-amylases and for trypsin inhibitors and that are dispersed over several chromosomes (11-15). Although the wheat monomeric and dimeric inhibitors have been extensively studied (16), less information is available concerning the tetrameric inhibitors (17)(18)(19). In particular, their subunits have not been purified ...

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“…Three main CM proteins (designated CM1 to CM3) are present in wheat and five (designated CMa to CMe) in barley [17,19,21]. They have similar MI values (about 12000-16000 by SDS-PAGE) and amino acid compositions.…”

Section: Resultsmentioning

confidence: 99%

“…Zephyr and tetraploid wheat (Triticum turgidurn) cv. Senatore Capelli respectively as described previously [ 17,191. CMd was also prepared, as was CM56, by ion-exchange chromatography and gel filtration of a reduced and pyridylethylated total hordein fraction from barley mutant Rise 56 [23].…”

Section: Methodsmentioning

confidence: 99%

N‐terminal amino acid sequences of chloroform/methanol‐soluble proteins and albumins from endosperms of wheat, barley and related species

et al. 1984

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The N-terminal amino acid sequences of two chloroform/methanol soluble globulins from barley and one form wheat are reported. They are homologous with N-terminal sequences previously reported for a-amylase and trypsin inhibitors from cereals and 2 S storage proteins from castor bean and rape. Three albumins were also purified from Aegilops squarrosa and Triticum monococcum. These had N-terminal amino acid sequences most closely related to the a-amylase and trypsin inhibitors. The relationships of this superfamily of seed proteins are discussed.

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Relationships among low MW hydrophobic proteins from wheat endosperm

Cited by 20 publications

References 11 publications

Genetics of CM-proteins (A-hordeins) in barley

Genetics of CM-proteins (A-hordeins) in barley

Wheat tetrameric inhibitors of insect α-amylases: Alloploid heterosis at the molecular level

N‐terminal amino acid sequences of chloroform/methanol‐soluble proteins and albumins from endosperms of wheat, barley and related species

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