Inheritance and mapping of storage protein genes in Pisum sativum L.

Matta, N. K.; Gatehouse, John A.

doi:10.1038/hdy.1982.51

Cited by 44 publications

(31 citation statements)

References 17 publications

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“…4, arrows). These differences can be expected among the various genera, in view of the variant subunit forms which have been observed intraspecifically, for example, with pea (12,23) and oat (17) globulins. Such variability might also be expected to contribute to heterogeneity at the holoprotein level as shown to exist in pea (24) and soybean (9,20).…”

Section: Discussionmentioning

confidence: 99%

Homology among 3S and 7S Globulins from Cereals and Pea

Robert

Adeli²,

Altosaar³

1985

Plant Physiol.

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The globulins from wheat caryopses were found to consist primarily of protein sedimenting at approximately 3S and 7S. These proteins displayed a molecular weight distribution similar to that of the purified vicilin-like fractions from oat and pea, with variations occurring in the isoelectric points and relative quantities of their major subunits. concanavalin A Sepharose chromatography suggested that the major polypeptides of the wheat (3S + 7S) fraction are glycosylated. Western blot analysis using antioat (3S + 7S) globulin immunoglobulin G revealed the vicilins from pea and the globulin fractions of oat, wheat, barley, rye, corn, and rice to contain immunologically homologous polypeptides. Major seed storage proteins of cereals and legumes generally exhibit a significant level of polypeptide microheterogeneity (6, 13). Part of this heterogeneity is believed to result from the duplication and mutational divergence of ancestral genes (10,21). Such divergence is apparently permitted because of the weaker function-related constraints imposed on the structure of storage proteins relative to that of other seed proteins such as enzymes ( 16).There are, however, limits to the evolutionary divergence of storage proteins which involve specific requirements for their recognition, processing, assembly, packaging, and degradation (6, 21). To reconcile both the existing laxity and stringency of the genetic controls involved, the observed heterogeneity might be accounted for by mutational changes permitted only in particular portions of the molecules. Examples of strong conservatism among seed storage proteins from legumes and cereals have been reported recently. These involved the two major classes of legume globulins, the legumin-like (I IS) and vicilin-like (3S and 7S) fractions, and specific seed proteins from oat and rice. The major component of the oat globulin fraction was shown to be a 12S globulin bearing a very close resemblance to legumin (3,4,11,17,26). The NH2-terminal amino acid sequences of the small basic subunits from oat 12S globulin and the I IS globulins from Glycine max, Vicia faba, and Pisum sativum were all reported to share considerable homology (26). Similar sequences obtained from the smaller subunits of pea legumin and a purified 22-kD rice glutelin polypeptide were also demonstrated to be homologous (27). The occurrence of legumin-like proteins in cereals may indicate that, similar to legumes, vicilin-like proteins are also present. Indeed, proteins displaying similar solubility characteristics, sedimentation values, mol wt, and glycosylation patterns to that of legume vicilins have already been observed in oat (1,4).In this paper, we report studies on the (3S + 7S) globulin fraction of wheat, and its homology to pea vicilins and to other cereal globulins.MATERIALS AND METHODS Plant Material. Mature seeds of oat (Avena saliva L. cv Hinoat), wheat (Triticum aestivum, cv Fredrick), rye (Secale cereale cv Puma), barley (Hordeum vulgare cv Perth), rice (Oryza sativa L. cv M-101), and corn (Ze...

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Section: Discussionmentioning

confidence: 99%

Homology among 3S and 7S Globulins from Cereals and Pea

Robert

Adeli²,

Altosaar³

1985

Plant Physiol.

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“…Marker afp9i is located 13 cM from the k gene, which was found by Matta and Gatehouse (1982) to be linked (approx. 3 cM) to a gene coding convicilin, a storage protein (Cvc).…”

Section: Individual Qtl Effectsmentioning

confidence: 99%

QTL for yield components and protein content: a multienvironment study of two pea (Pisum sativum L.) populations

et al. 2011

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Quantitative trait loci for yield, yield components and seed protein content were investigated on the basis of experiments performed with two populations of pea (Pisum sativum L.) lines derived from linked crosses between lines Wt11238, Wt3557 and Wt10245 with contrasting characteristics. The yield-related traits were defined as components giving the grain yield in a multiplicative way. The aim was to clarify the genetic architecture of the relation between seed yield, its components and protein content, with a possible inclusion of the role of epistasis in this explanation. To take full advantage of the availability of the two populations, additive QTL effects and both types of epistasis were analysed: the QTL by genetic background interaction and the first-order QTL-QTL interaction. The two hybrid populations differed with respect to the prevailing gene action, which in the Wt11238 9 Wt3557 progeny was mainly additive, while in the Wt10245 9 Wt11238 progeny mainly epistatic. Some loci with previously reported, large, repeatable, but contradictory effects on yield and protein content were confirmed. New loci with alleles coming from the protein-rich Wt11238 line, positive for yield components, were identified. It was found that the first order QTL-QTL interaction events were more frequent for the loci showing the QTL by genetic background interaction.

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“…Elucidation of the synthesis of vicilin has shown that the initial products of the vicilin structural genes are 50,000 Mr precursors, of differing amino acid sequences, some of which are proteolytically cleaved after translation is complete to yield the "subunits" or component polypeptides of Mr < 35,000 observed in the protein as isolated (Gatehouse et a!., , 1982. Variation in the 50,000 Mr subunits of vicilin is thus most likely to reflect variation in the structural genes for the protein rather than to be a result of post-translational modification (which may not be simply related to protein structure).…”

Section: Introductionmentioning

confidence: 99%

“…Lg-1) (Davies, 1980); Matta and Gatehouse, 1982). The latter authors also reported the mapping of the genetic locus for the storage protein related to vicilin, convicilin (Cvc), to a segment of chromosome 2 on the pea genome (s. 18• Cvc 3 k) where s is the locus determining "sticky" (s) or "non-sticky" (S) seeds ("sticky" seeds adhere together in the pod), and k is the locus determining normal (K) or keel-like (k) wings on the flowers.…”

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confidence: 99%

Inheritance and mapping of vicilin storage protein genes in Pisum Sativum L

Mahmoud

Gatehouse

1984

Heredity

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SUMMARYGel electrophoresis techniques have been used to investigate genetically controlled variation in the major subunits (Mr 50,000) of vicilin, a storage protein of Pisum sativum L. The F1 protein band patterns were shown to be additive with respect to those of the parental lines and to be identical in reciprocal crosses. Genetic analysis of the F2 plants indicated that the 50,000 Mr vicilin subunit band pattern is controlled by a pair of co-dominant genes at single locus. The F2 data were used to locate this major vicilin gene locus (Vc-l) to chromosome 7, closely linked to the r locus (for round and wrinkled seed surface).

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Inheritance and mapping of storage protein genes in Pisum sativum L.

Cited by 44 publications

References 17 publications

Homology among 3S and 7S Globulins from Cereals and Pea

Homology among 3S and 7S Globulins from Cereals and Pea

QTL for yield components and protein content: a multienvironment study of two pea (Pisum sativum L.) populations

Inheritance and mapping of vicilin storage protein genes in Pisum Sativum L

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