Identification of AFLP Markers Tightly Linked to the Gene for Deficiency of the 7S Globulin in Soybean Seed and Characterization of Abnormal Phenotypes Involved in the Mutation.

The bolting time of varieties used as leafy vegetables or turnips within the Brassica rapa (syn. campestris) species is important, because it affects the yield and quality of the harvested products. In Brassica rapa, the transition from the vegetative to reproductive phase is influenced by environmental factors, such as daylength and low temperature. In order to analyze the genetic basis of bolting time, an AFLP linkage map was constructed using doubled haploid (DH) lines derived from the F 1 hybrid between A9408 and Homei P09. QTL analysis of bolting time was performed based on the evaluation under two field conditions and three artificial conditions differing in day-length and/or temperature. Out of a total of ten QTLs detected, two QTLs showed a low temperature sensitivity. The most effective QTL, BT1, was found to be the main locus controlling the vernalization response and the allele of Homei P09 was highly responsive to low temperature compared with that of the late parent A9408. These results could be useful for marker-assisted selection and isolation of the genes responsible for bolting time in Brassica rapa.

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“…AFLP protocol was adopted essentially as described by Vos et al (1995) with minor modifications according to the mehod of Hayashi et al (2000).…”

Section: Aflp Analysismentioning

confidence: 99%

Mapping of QTLs for Bolting Time in Brassica rapa (syn. campestris) under Different Environmental Conditions

et al. 2005

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“…However, the cgdef mutant line has adverse characteristics such as morphological abnormality and lethality, which are not suitable for breeding. In a subsequent study, the abnormal phenotypes were found to be closely linked but independent of b-conglycinin deficiency (Hayashi et al 2000). The cgdef gene was mapped in linkage group (LG) L/Gm19 between simple sequence repeat (SSR) markers Satt523 and Sat_388 (Hayashi et al 2009).…”

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The β-conglycinin deficiency in wild soybean is associated with the tail-to-tail inverted repeat of the α-subunit genes

Tsubokura

Hajika

Kanamori³

et al. 2011

Plant Mol Biol

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β-conglycinin, a major seed protein in soybean, is composed of α, α', and β subunits sharing a high homology among them. Despite its many health benefits, β-conglycinin has a lower amino acid score and lower functional gelling properties compared to glycinin, another major soybean seed protein. In addition, the α, α', and β subunits also contain major allergens. A wild soybean (Glycine soja Sieb et Zucc.) line, 'QT2', lacks all of the β-conglycinin subunits, and the deficiency is controlled by a single dominant gene, Scg-1 (Suppressor of β-conglycinin). This gene was characterized using a soybean cultivar 'Fukuyutaka', 'QY7-25', (its near-isogenic line carrying the Scg-1 gene), and the F₂ population derived from them. The physical map of the Scg-1 region covered by lambda phage genomic clones revealed that the two α-subunit genes, a β-subunit gene, and a pseudo α-subunit gene were closely organized. The two α-subunit genes were arranged in a tail-to-tail orientation, and the genes were separated by 197 bp in Scg-1 compared to 3.3 kb in the normal allele (scg-1). In addition, small RNA was detected in immature seeds of the mutants by northern blot analysis using an RNA probe of the α subunit. These results strongly suggest that β-conglycinin deficiency in QT2 is controlled by post-transcriptional gene silencing through the inverted repeat of the α subunits.

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“…Hayashi et al (11) used amplified fragment length polymorphism markers to locate the cgdef locus in soybean. This locus determines the β-conglycinin content in soybean, and a single recessive gene reduces the β-conglycinin content.…”

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Quantitative trait loci for β‐conglycinin (7S) and glycinin (11S) fractions of soybean storage protein

Panthee

Kwanyuen

Sams

et al. 2004

J Americ Oil Chem Soc

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Glycinin (11S) and β-conglycinin (7S) are important seed storage proteins in soybean [Glycine max (L.) Merr.].A major limitation of soybean seed storage proteins is their low levels of the sulfur-containing amino acids, methionine and cysteine, which are important nutritional components of protein meal. Glycinin contains significantly more S-containing amino acids than does β-conglycinin. Thus, detection of quantitative trait loci (QTL) that govern 11S may provide marker-assisted selection (MAS) opportunities to improve soybean total S-containing amino acids. The objective of this study was to detect and map QTL governing 7S and 11S fractions of soybean seed storage proteins. To achieve this objective, 101 F 6 -derived recombinant inbred lines (RIL) developed from a cross of N87-984-16 × TN93-99 were used. Storage proteins were extracted from all RIL and separated in 10-20% linear gradient polyacrylamide gels. Dried gels were scanned for individual subunits of storage protein with a densitometer equipped with a He-Ne laser light source. Data were converted to concentration for each subunit component and analyzed using SAS software. A significant (P < 0.05) difference among genotypes was found for glycinin and β-conglycinin. A total of 94 polymorphic simple sequence repeat molecular genetic markers were used in screening all RIL. Three QTL for glycinin (Satt461, Satt292, and Satt156) were distributed on linkage group (LG) D2, I, and L, respectively, whereas two QTL for conglycinin (Satt461 and Satt249) were distributed on LG D2 and J. Phenotypic variation explained by individual QTL ranged from 9.5 to 22%. These QTL may provide useful MAS opportunities for improvement of nutritional quality in soybean.Soybean is a major source of protein and amino acids for human and animal feeds in the world (1). However, soy protein is not perfect because of its low levels of the sulfur-containing essential amino acids, methionine and cysteine. Enhancing the concentration of nutritionally essential amino acids in soybean would improve soy meal quality and boost its inclusion in diets for humans and animals.Soybean storage protein has two major fractions, β-conglycinin (7S) and glycinin (11S), accounting for more than 70% of the total proteins (2). β-Conglycinin is a trimer with subunits α, α′, and β, and a M.W. of about 180 kDa. Glycinin is a hexamer with a M.W. of 360 kDa, consisting of acidic and basic subunits. Glycinin constitutes about 35% of the total seed storage protein (3). Glycinin has three to four times more S-containing amino acids (particularly methionine) than does β-conglycinin (4). In addition, the β subunit of conglycinin is known to be void of methionine and cysteine. Hence, the glycinin fraction may be more desirable than the β-conglycinin fraction in developing improved amino acid balance in soy meal. Both 7S and 11S are components of total seed protein, and there is a typical inverse relationship between 7S and 11S concentrations (5). Thus, glycinin can be increased at the expense of β-conglycinin. Mutants ...

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Identification of AFLP Markers Tightly Linked to the Gene for Deficiency of the 7S Globulin in Soybean Seed and Characterization of Abnormal Phenotypes Involved in the Mutation.

Cited by 17 publications

References 38 publications

Mapping of QTLs for Bolting Time in Brassica rapa (syn. campestris) under Different Environmental Conditions

Mapping of QTLs for Bolting Time in Brassica rapa (syn. campestris) under Different Environmental Conditions

The β-conglycinin deficiency in wild soybean is associated with the tail-to-tail inverted repeat of the α-subunit genes

Quantitative trait loci for β‐conglycinin (7S) and glycinin (11S) fractions of soybean storage protein

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