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  • Author or Editor: Yan Wang x
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Genetic structure of 142 parent lines of sorghum [Sorghum bicolor (L.) Moench] was analyzed using model-based approach based on SSR markers. Forty-one selected from 103 SSR markers were used to analyze the parent lines, which generated 189 alleles revealed by each marker ranging from 2 to 11 with an average of 4.6 per marker. The polymorphic information content (PIC) value was 0.543 with a range of 0.089 to 0.850. All the parent lines were assigned to 7 subgroups, named Kafir, Kaoliang, Feterita, Shallu, Hegari, Milo and Durra. Parent lines without clear pedigree record were clustered into their corresponding groups, and genetic components of each line were estimated by Q-values. Information of this study would be useful for breeders to conclude their genetic background and select appropriate parents for germplasm improvement and hybrid breeding, and thus improve the efficiency of breeding programs.

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The wheat storage proteins, especially the high molecular weight glutenin subunits (HMW-GS), play important roles in the determination of flour processing and bread-making quality. Compared with the traditional SDS-PAGE method, reversed-phase high-performance liquid chromatography (RP-HPLC) was shown to have many advantages for the separation and characterization of HMW-GS because of its high resolving power, repeatability and automation. In this work, HMW-GS from bread and tetraploid wheats were separated and characterized by RP-HPLC. The elution time ranking of different HMW-GS was: 1Ax > 1Bx > 1Dx > 1By > 1Dy. Several subunit pairs associated with good quality properties and those with similar mobilities on SDS-PAGE, such as 1Bx7 and 1Bx7*, 1By8 and 1By8*, 1Dx2 and 1Ax2*, 1Bx6 and 1Bx6.1, were well separated and readily identified through RP-HPLC. However, other subunit pairs, such as 1Dy10 — 1Dy12, 1Dx5 — 1By18 and 1Dx2 — 1By16, could not be adequately separated and identified by RP-HPLC, whereas they displayed different mobilities on SDS-PAGE gels. Because 1Dx5 and 1Dx2 showed different hydrophobicities, RP-HPLC could distinguish 1Dx5 + 1Dy10 and 1Dx2 + 1Dy12. A comparative analysis between RP-HPLC and SDS-PAGE showed that a combination of both methods provided more effective identification of HMW-GS in wheat quality improvement and germplasm screening.

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Fructose-bisphosphate aldolase (FBA, EC 4.1.2.13) catalyzes an aldol cleavage of fructose-1, 6-bisphosphate to dihydroxyacetone-phosphate and glyceraldehyde 3-phosphate and a reversible aldol condensation. Three candidate genes with 1077bp coding for fructose-bisphosphate aldolase were cloned and sequenced in wheat, barley and rye. These genes could encode 358 amino acid residues. Sequence analysis indicated that wheat, barley and rye FBA genes were conserved with high identity (94.13%), while maize sequence had a 9bp deletion near the 3’ terminal. According to the alignment of 75 amino acid sequences, conserved domains of the FBAs were detected. These conserved domains might be the important functional sites of the FBAs. The cytoplasmic FBAs of wheat, barley and rye were clustered together, and the cluster was close to maize and rice FBAs. Nine peptides of the FBAs and the last amino acid Tyr (necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate) were most conserved in plants, animals and algae. Current findings suggested that the FBAs could be divided into three main subgroups: plant cytoplasmic FBA, plant chloroplastic FBA and animal FBA. These results also indicated that the active and binding sites of FBAs had rare variations during the long-term evolution.

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Two new y-type HMW-GSs in Ae. tauschii , 1Dy12.1* t and 1Dy12.2 t with the mobility order of 1Dy12.2 t > 1Dy12.1* t > 1Dy12.1 t >1Dy12, were identified by both SDS-PAGE and MALDI-TOF-MS. Molecular cloning and sequencing showed that the genes encoding subunits 1Dy12.1* t and 1Dy12.2 t had identical nucleotide acid sequences with 1,947 bp encoding a mature protein of 627 residues. Their deduced molecular weights were 67,347.6 Da, satisfactorily corresponding to that of 1Dy12.2 t subunit determined by MALDI-TOF-MS (67,015.7 Da), but was significantly smaller than that of the the 1Dy12.1* t subunit (68,577.1 Da). Both subunits showed high similarities to 1Dy10, suggesting that they could have a positive effect on bread-making quality. Interestingly, the expressed protein of the cloned ORF from accessions TD87 and TD130 in E. coli co-migrated with subunit 1Dy12.2 t , but moved slightly faster than 1Dy12.1* t on SDS-PAGE. The expressed protein in transgenic tobacco seeds, however, had the same mobility as the 1Dy12.1* t subunit, as confirmed by both SDS-PAGE and Western blotting. Although direct evidence of phosphoprotein could not be obtained by specific staining method, certain types of post-translational modifications (PTMs) of the 1Dy12.1* t subunit could not be excluded. We believe PTMs might be responsible for the molecular weight difference between the subunits 1Dy12.1* t and 1Dy12.2 t .

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A comparative proteomic analysis of grain proteins during five grain developmental stages of wheat cultivar Chinese Spring (CS) and its 1Sl/1B substitution line CS-1Sl(1B) was carried out in the current study. A total of 78 differentially expressed protein (DEP) spots with at least 2-fold expression difference were detected by two-dimensional electrophoresis (2-DE). Among these, 73 protein spots representing 55 differentially expressed proteins (DEPs) were successfully identified by matrix-assisted laser desorption/ionization time-offlight tandem mass spectrometry (MALDI-TOF/TOF-MS). Differential protein spots between the two genotypes were analyzed by cluster software, which revealed significant proteome differences. There were 39 common spots (including 33 DEPs) that showed significant difference between the two lines across five grain developmental stages, of which 14 DEP spots (including 11 DEPs) were mainly involved in carbohydrate metabolism that were encoded by the genes on 1B chromosome while 25 DEP spots (including 12 DEPs) were mainly related to stress response and gluten quality that were encoded by 1S1 chromosome. These results indicated that the Sl genome harbors more stress and quality related genes that are potential valuable for improving wheat stress resistance and product quality.

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Xinjiang rice wheat ( Triticum petropavlovskyi Udacz. et Migush, 2n=6x=42, AABBDD) is one of the endemic Chinese wheats, only distributing in Xinjiang and Xizang (Tibet), China. A novel high-molecular-weight (HMW) glutenin subunit gene 1Dx2.1 was isolated and characterized from Xinjiang rice wheat accession Daomai2. The complete open reading frame (ORF) of 1Dx2.1 is 2508 bp, encoding 836 amino acids. The primary structure of 1Dx2.1 consists of three distinct domains, a non-repetitive N-terminal domain with 89 residues, a non-repetitive C-terminal domain with 42 residues and a large central repetitive domain with 684 residues. In the N-terminal of 1Dx2.1, there is an R (arginine) at position 75, whereas there is a Q (glutamine) in other known x-type subunits. Four cysteine residues are observed in 1Dx2.1 with three in the N-terminal region and one in the C-terminal region. The number and distribution of cysteines in 1Dx2.1 are identical to those in x-type subunits except for 1Dx5, which possesses an extra cysteine residue. Differences between the repetitive domain of 1Dx2.1 and those of known HMW subunits resulted from substitutions, insertions or/and deletions involving single or more amino acid residues. The phylogenetic tree, which was constructed on the basis of amino acid sequences, and indicated that 1Dx2.1 was highly related to 1Dx2.1 t , then to 1Dx2 and 1Dx5.

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New high-molecular-weight glutenin (HMW glutenin) sequences isolated from six Psathyrostachys juncea accessions by thermal asymmetric interlaced PCR differ from previous sequences from this species. They showed novel modifications in all of the structural domains, with unique C-terminal residues, and their N-terminal lengths were the longest among the HMW glutenins reported to date. In their repetitive domains, there were three repeatable motif units: 13-residue [GYWH(/I/Y)YT(/Q)S(/T)VTSPQQ], hexapeptide (PGQGQQ), and tetrapeptide (ITVS). The 13-residue repeats were restricted to the current sequences, while the tetrapeptides were only shared by D-hordein and the current sequences. However, these sequences were not expressed as normal HMW glutenin proteins because an in-frame stop codon located in the C-termini interrupted the intact open reading frames. A phylogenetic analysis supported different origins of the P. juncea HMW glutenin sequences than that revealed by a previous study. The current sequences showed a close relationship with D-hordein but appeared to be more primitive.

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Cereal Research Communications
Authors:
W.T. Xue
,
A. Gianinetti
,
R. Wang
,
Z.J. Zhan
,
J. Yan
,
Y. Jiang
,
T. Fahima
,
G. Zhao
, and
J.P. Cheng

Crop seeds are the main staples in human diet, especially in undeveloped countries. In any case, the diet needs to be rich not only in macro-nutrients like carbohydrates and protein, but also in micro-nutrients. Nevertheless, both the macro- and micro-nutrients presented in seeds largely vary in consequence of field and environment conditions. In this research, 60 lines of a barley RILs population segregating for the SSR marker Hvm74, which is genetically linked to the GPC (grain protein content) locus (HvNAM-1), were studied in 4 environments (two growing years and two field managements) by carrying out a comprehensive profile of seed macro- (starch, total nitrogen and total soluble protein) and micro-nutrients (phytate, phenolics, flavonoids, Pi, Zn and Fe). Under field conditions, all the components were largely affected by the environment, but TN (total nitrogen) exhibited high genotype contribution, while micro-nutrients displayed higher genotype × environments interactions (GEI) than macro-nutrients. In order to approach the effects of carbon-nitrogen (C–N) balance on other seed components, two C/N ratios were calculated: C/TN (CNR1) and C/TSP (CNR2). CNR2 exhibited stronger negative correlations with all micro-nutrients. Hence, the significant GEI and its negative relationships with CNR2 highlighted the different characters of micro-nutrients in barley seeds.

Open access
Cereal Research Communications
Authors:
S. Wang
,
D. Chen
,
G. Guo
,
T. Zhang
,
S. Jiang
,
X. Shen
,
D. Perovic
,
S. Prodanovic
, and
Y. Yan

In this work, 9 novel LMW-GS genes (6 LMW-m and 3 LMW-i type) from 4 diploid and 1 tetraploid Aegilops species were amplified and cloned by allelic-specific PCR. Analysis of the deduced amino acid sequences showed that 7 and 2 LMW-GS had 9 and 7 cysteines, respectively. Four LMW-m type subunits genes had an extra cysteine at the C-terminal III, which could form intermolecular disulphide bonds to extend the chains, and therefore would facilitate to form larger gluten polymers. This suggested that these genes are expected to be used as candidate genes for wheat quality improvement. The correlation between specific N-terminal sequences and a decapeptide deletion in the C-terminal II in LMW-GS encoded by D genome was found. Particularly, if LMW-GS possessed a METRCIPG-N-terminal beginning sequences and a decapeptide (LGQCSFQQPQ) deletion in the C-terminal II, they could be encoded by D genome.

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