New insights into the evolution of wheat avenin-like proteins in wild emmer wheat (
            <i>Triticum dicoccoides</i>
            )

Zhang, Yujuan; Hu, Xin; Islam, Shahidul; She, Maoyun; Peng, Yanchun; Yu, Zitong; Wylie, Stephen J.; Juhász, Angéla; Dowla, Mirza; Yang, Rongchang; Zhang, Jingjuan; Wang, Xiaolong; Dell, B.; Chen, Xueyan; Nevo, Eviatar; Sun, Dongfa; Ma, Wujun

doi:10.1073/pnas.1812855115

Cited by 35 publications

(37 citation statements)

References 46 publications

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“…Mutations or silencing of such genes are not lethal for the plant, so the evolutionary selection pressure on these genes is much lower than for functional genes [6] . As a result, these genes can accumulate more mutations, making them ideal model molecules for studying a range of biological fundamental processes [7][8][9][10] . It is worth noting that past work has been primarily focused on the applied aspects of using these proteins to increase wheat end product quality.…”

Section: Wheat Gluten Protein Variationsmentioning

confidence: 99%

“…Their value in theoretical research has been largely ignored. So far, only Zhang et al [8] has reported a biological function other than the storage function for gluten, an antifungal function of a newly identified special gluten protein, namely aveninlike protein, which is quite similar to the gliadins in structure. Until now, extensive studies have provided substantial information about the relationship between gluten structures and properties in relation to end product quality.…”

Section: Wheat Gluten Protein Variationsmentioning

confidence: 99%

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Wheat gluten protein and its impacts on wheat processing quality

She

et al. 2019

Front. Agr. Sci. Eng.

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Before the advent of the wheat genomic era, a wide range of studies were conducted to understand the chemistry and functions of the wheat storage proteins, which are the major determinants of wheat flour the suitability of wheat flour for various end products, such as bread, noodles and cakes. Wheat grain protein is divided into gluten and non-gluten fractions and the wheat processing quality mainly depends on the gluten fractions. Gluten provides the unique extensibility and elasticity of dough that are essential for various wheat end products. Disulfide bonds are formed between cysteine residues, which is the chemical bases for the physical properties of dough. Based on the SDS-extractability, grain protein is divided into SDS-unextractable polymeric protein (UPP) and SDS-extractable polymeric protein. The percentage of UPP is positively related to the formation of disulfide bonds in the dough matrix. In the wheat genomic era, new glutenins with long repetitive central domains that contain a high number of consensus hexapeptide and nonapeptide motifs as well as high content of cysteine and glutamine residues should be targeted.

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Section: Wheat Gluten Protein Variationsmentioning

confidence: 99%

Section: Wheat Gluten Protein Variationsmentioning

confidence: 99%

Wheat gluten protein and its impacts on wheat processing quality

She

et al. 2019

Front. Agr. Sci. Eng.

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“…Improvements in wheat DH production have resulted from co-culture with ovaries [11] and n-butanol treatment [12,13]. Approximately 90% of the DH lines developed in our program are destined for plant breeding companies, with the remaining populations used for research projects throughout Australia [14,15]. Genotype variability in key production parameters, such as embryo production, green plant regeneration and chromosome doubling, is an ongoing challenge, especially for the high-throughput production of breeding populations.…”

Section: Introductionmentioning

confidence: 99%

The Effect of Caffeine and Trifluralin on Chromosome Doubling in Wheat Anther Culture

Broughton

Castello

Liu

et al. 2020

Plants

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Challenges for wheat doubled haploid (DH) production using anther culture include genotype variability in green plant regeneration and spontaneous chromosome doubling. The frequency of chromosome doubling in our program can vary from 14% to 80%. Caffeine or trifluralin was applied at the start of the induction phase to improve early genome doubling. Caffeine treatment at 0.5 mM for 24 h significantly improved green plant production in two of the six spring wheat crosses but had no effect on the other crosses. The improvements were observed in Trojan/Havoc and Lancer/LPB14-0392, where green plant numbers increased by 14% and 27% to 161 and 42 green plants per 30 anthers, respectively. Caffeine had no significant effect on chromosome doubling, despite a higher frequency of doubling in several caffeine treatments in the first experiment (67–68%) compared to the control (56%). In contrast, trifluralin significantly improved doubling following a 48 h treatment, from 38% in the control to 51% and 53% in the 1 µM and 3 µM trifluralin treatments, respectively. However, trifluralin had a significant negative effect on green plant regeneration, declining from 31.8 green plants per 20 anthers (control) to 9–25 green plants per 20 anthers in the trifluralin treatments. Further work is required to identify a treatment regime with caffeine and/or anti-mitotic herbicides that consistently increases chromosome doubling in wheat without reducing green plant regeneration.

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“…In wheat, the ALPs can be detected in the gluten-enriched fraction, including among others a range of gliadins, glutenins, protease inhibitors and LTPs [44]. The ALPs were named due to sequence homology with avenins of oats [45], most closely to avenin-3 [46], and α-, γ-gliadins [47]. Kasarda et al [48] characterized a novel ALP called farinin, composed by two disulphide-linked small polypeptides subsequent to a proteolytic cleavage of a precursor polypeptide at an Asn-Glu (N-E) peptide bond.…”

Section: Introductionmentioning

confidence: 99%

“…Based on the study by Altenbach et al [55], the farinins (ALPs) comprised from 2.6 to 3.1% of the protein in the SDS-extractable polymeric proteins (EPP) and 1.9-2.4% of the protein in the SDS-unextractable polymeric proteins (UPP), and they were influenced by post-anthesis fertilizer. Both type b subunits (bx and by) of ALPs were reported to have non-functional pseudogenes in Brachypodium distachyon L accessions, Triticum dicoccoides, and T. aestivum [47,56]. Most recently, more novel alleles of ALP were found in Aegilops tauschii Coss.…”

Section: Introductionmentioning

confidence: 99%

Characterising avenin-like proteins (ALPs) from albumin/globulin fraction of wheat grains by RP-HPLC, SDS-PAGE, and MS/MS peptides sequencing

Zhang

Juhász

et al. 2020

BMC Plant Biol

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Background: Wheat grain avenin-like proteins (ALPs) belong to a recently discovered class of wheat grain storage protein. ALPs in wheat grains not only have beneficial effects on dough quality but also display antifungal activities, which is a novel observation for wheat storage proteins. Previous studies have shown that ALPs are likely present in the albumin/globulin fractions of total protein extract from wheat flour. However, the accumulation characteristics of these ALPs in the mature wheat grain remains unknown. Results: In the present study, a total of 13 ALPs homologs were isolated and characterized in the albumin/globulin fractions of the wheat protein extract. A combination of multiple techniques including RP-HPLC, SDS-PAGE, MALDI-TOF and peptide sequencing were used for accurate separation and identification of individual ALP homolog. The C-terminal TaALP-by-4AL/7DS, TaALP-by-4AL/7AS/7DS, TaALP-bx/4AL/7AS/7DS, TaALP-ay-7DS, TaALP-ay-4AL, TaALPax-4AL, TaALP-ax-7AS, and TaALP-ax-7DS, were separated as individual protein bands from wheat flour for the first time. These unique ALPs peptides were mapped to the latest wheat genome assembly in the IWGSC database. The characteristic defence related proteins present in albumin and globulin fractions, such as protein disulfide-isomerase (PDI), grain softness protein (GSP), alpha-amylase inhibitors (AAIs) and endogenous alpha-amylase/subtilisin inhibitor were also found to co-segregate with these identified ALPs, avenin-3 and α-gliadins. The molecular weight range and the electrophoresis segregation properties of ALPs were characterised in comparison with the proteins containing the tryp_alpha_amyl domain (PF00234) and the gliadin domain (PF13016), which play a role in plant immunity and grain quality. We examined the phylogenetic relationships of the AAIs, GSP, avenin-3, α-gliadins and ALPs, based on the alignment of their functional domains. MALDI-TOF profiling indicated the occurrence of certain post-translations modifications (PTMs) in some ALP subunits. Conclusions: We reported for the first time the complete profiling of ALPs present in the albumin/globulin fractions of wheat grain protein extracts. We concluded that majority of the ALPs homologs are expressed in wheat grains. We found clear evidence of PTMs in several ALPs peptides. The identification of both gliadin domain (PF13016) and Tryp_alpha_amyl domain (PF00234) in the mature forms of ALPs highlighted the multiple functional properties of ALPs in grain quality and disease resistance.

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New insights into the evolution of wheat avenin-like proteins in wild emmer wheat ( Triticum dicoccoides )

Cited by 35 publications

References 46 publications

Wheat gluten protein and its impacts on wheat processing quality

Wheat gluten protein and its impacts on wheat processing quality

The Effect of Caffeine and Trifluralin on Chromosome Doubling in Wheat Anther Culture

Characterising avenin-like proteins (ALPs) from albumin/globulin fraction of wheat grains by RP-HPLC, SDS-PAGE, and MS/MS peptides sequencing

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