Comparison of orthologous and paralogous DNA flanking the wheat high molecular weight glutenin genes: sequence conservation and divergence, transposon distribution, and matrix-attachment regions

Genome ◽  
2002 ◽  
Vol 45 (2) ◽  
pp. 367-380 ◽  
Author(s):  
O D Anderson ◽  
L Larka ◽  
M J Christoffers ◽  
K F McCue ◽  
J P Gustafson
Keyword(s):  
Molecular Weight ◽  
Transposable Elements ◽  
High Molecular Weight ◽  
Dna Sequences ◽  
Binding Activity ◽  
Sequence Conservation ◽  
Matrix Attachment Regions ◽  
Coding Region ◽  
Hmw Glutenin ◽  
Miniature Inverted Transposable Elements

Extended flanking DNA sequences were characterized for five members of the wheat high molecular weight (HMW) glutenin gene family to understand more of the structure, control, and evolution of these genes. Analysis revealed more sequence conservation among orthologous regions than between paralogous regions, with differences mainly owing to transposition events involving putative retrotransposons and several miniature inverted transposable elements (MITEs). Both gyspy-like long terminal repeat (LTR) and non-LTR retrotransposon sequences are represented in the flanking DNAs. One of the MITEs is a novel class, but another MITE is related to the maize Stowaway family and is widely represented in Triticeae express sequence tags (ESTs). Flanking DNA of the longest sequence, a 20 425-bp fragment including and surrounding the HMW-glutenin Bx7 gene, showed additional cereal gene-like sequences both immediately 5' and 3' to the HMW-glutenin coding region. The transcriptional activities of sequences related to these flanking putative genes and the retrotransposon-related regions were indicated by matches to wheat and other Triticeae ESTs. Predictive analysis of matrix-attachment regions (MARs) of the HMW glutenin and several α-, γ-, and ω-gliadin flanking DNAs indicate potential MARs immediately flanking each of the genes. Matrix binding activity in the predicted regions was confirmed for two of the HMW-glutenin genes.Key words: wheat, glutenins, evolution, matrix-attachment regions, transposable elements.

Intraindividual Comparison of the Impact of two Selective Apheresis Methods (DALI and HELP) on the Coagulation System

2000 ◽  
Vol 23 (3) ◽  
pp. 199-206 ◽  
Author(s):  
U. Julius ◽  
G. Siegert ◽  
S. Gromeier
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Protein S ◽  
Binding Activity ◽  
Coagulation System ◽  
Factor Xii ◽  
High Molecular Weight Kininogen ◽  
Prothrombin Fragment ◽  
Intraindividual Comparison ◽  
The Impact

We performed an intraindividual comparison of the effect on the coagulation system of two selective apheresis procedures: Direct Adsorption of Lipoproteins (DALI) and Heparin-induced Lipoprotein Fibrinogen Precipitation (HELP). Six patients suffering from heterozygous familial hypercholesterolemia have been treated with 2 sessions of each procedure. Anticoagulation was carried out according to usual recommendations. Blood samples were taken before, immediately after and on the second day after the sessions. We assessed global coagulation tests (prothrombin time, activated partial thromboplastin time), fibrinogen, prothrombin fragment F 1 + 2 and a variety of factors (Factors II, V, VII, XIII, IX, X, XI, XII, XIIa; von Willebrand Factor; collagen-binding activity, prekallikrein, high-molecular weight kininogen) and antagonists (antithrombin III, protein S activity, free protein S). In fact, all parameters measured have been influenced by the apheresis treatment. Fibrinogen is lowered more by HELP, which also has a more definite impact on factors belonging to the prothrombin complex (II, VII, X). In contrast, the major effects of the DALI system have been seen on the intrinsic pathway of the coagulation system (IX, XI, prekallikrein, high-molecular-weight kininogen). With both systems, no increases in activated Factor XII or in prothrombin fragment F1 + 2 have been observed. These data provide a solid basis for individual adaptations of anticoagulant doses.

The association between high molecular weight glutenin subunit compositions and the bread-making quality of Chinese and Japanese hexaploid wheats

2000 ◽  
Vol 51 (3) ◽  
pp. 371 ◽  
Author(s):  
H. Nakamura
Keyword(s):  
Molecular Weight ◽  
Genetic Variation ◽  
High Molecular Weight ◽  
Hexaploid Wheat ◽  
Allelic Variation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Glutenin Subunit ◽  
Wheat Varieties ◽  
Hmw Glutenin

Variation in the electrophoretic banding patterns of high molecular weight (HMW) glutenin subunits of 274 hexaploid wheat (Triticum aestivum) varieties from China was examined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Twenty-seven different major glutenin HMW subunits were identified. Each variety contained 3–5 subunits and 29 different glutenin subunit patterns were segregated. Seventeen alleles were identified based on comparison of subunit mobilities with those previously found for hexaploid wheat. Chinese hexaploid wheats exhibited particular allelic variation in glutenin HMW subunit composition and this variation differed from that found in wheats from Japanese and other countries. Average Glu-1 quality scores of 274 Chinese wheat varieties in the present study have been shown to be higher than that of Japanese wheats. Considerable genetic variation in the HMW glutenin subunit compositions of the Chinese wheats was observed in the present study and previously. Alleles from Chinese hexaploid wheat varieties have not been extensively introduced into Japan and other countries. The present data may indicate possible applications of Chinese germplasm in wheat breeding programs. To improve the wheat quality, genetic variation should be attempted through the introduction of genes of Chinese varieties into varieties in Japan and other countries.

scholarly journals Cloning and characterization of high molecular weight glutenin gene from Triticum aestivum cultivar Dacke

2018 ◽  
Vol 4 (10) ◽  
pp. 254
Author(s):  
Kirushanthy Kajendran ◽  
Naduviladath Vishvanath Chandrasekharan ◽  
Chamari Madhu Hettiarachchi ◽  
Wijerupage Sandhya Sulochana Wijesundera
Keyword(s):  
Molecular Weight ◽  
Triticum Aestivum ◽  
Sequence Analysis ◽  
High Molecular Weight ◽  
Repetitive Domain ◽  
Milling Quality ◽  
Reading Frame ◽  
Calculated Molecular Weight ◽  
Hmw Glutenin ◽  
Glutenin Protein

<p class="abstract"><strong>Background:</strong> High molecular weight (HMW) glutenin protein plays a crucial role in determining dough viscoelastic properties that determines the quality of wheat flour. The aim of the present study was to isolate, clone and analyze (<em>in silico</em>) the HMW glutenin gene of <em>Triticum aestivum</em> cultivar Dacke.</p><p class="abstract"><strong>Methods:</strong> Primers were designed to amplify a 2445 bp fragment of HMW glutenin gene. Ax type HMW glutenin gene from <em>Triticum aestivum</em> cultivar Dacke was isolated using PCR and it was sequenced by primer walking.  </p><p class="abstract"><strong>Results:</strong> Amplified HMW glutenin gene was designated as HMWGAx. Sequence analysis revealed a complete open reading frame encoding 815 amino acid residues with N- and C terminal non-repetitive domain and a central repetitive domain. The calculated molecular weight of the deduced HMW glutenin protein was ~88 kDa and the number of cysteine residues in the HMWGAx was four, in accordance with other x type HMW glutenin proteins. Phylogenetic analysis revealed 100% homology to the previously studied Ax2* type HMW glutenin gene from cultivar Cheyenne. Predicted secondary structure results showed that it was similar to1Ax1 type of common wheat (<em>Triticum aestivum</em>), having superior flour milling quality.</p><p><strong>Conclusions:</strong> Sequence analysis suggests that HMWGAx protein significantly and positively correlates with the properties of elasticity and extensibility of gluten. </p>

scholarly journals Polymorphism of high-molecular-weight glutenin loci in Ukrainian wheat landraces Triticum aestivum L.

2021 ◽  
Vol 29 ◽  
pp. 111-116
Author(s):  
T. O. Sobko ◽  
G.M. Lisova ◽  
O.M. Blagodarova
Keyword(s):  
Molecular Weight ◽  
Triticum Aestivum ◽  
Winter Wheat ◽  
High Molecular Weight ◽  
Gene Pool ◽  
Allelic Diversity ◽  
Triticum Aestivum L ◽  
Hmw Glutenin ◽  
Wheat Landraces ◽  
In The Beginning

Aim. The aim of the study was to investigate allelic variability of high-molecular-weight glutenin loci Glu-A1, Glu-B1, Glu-D1 in Ukrainian winter wheat landraces and obsolete cultivars Triticum aestivum L. Methods. Allelic diversity at the Glu-1 loci were analyzed in 54 collection accessions, including 41 landraces (Krymka, Banatka, Girka, Theyka and others), and 13 first breeding cultivars that were developed in the beginning of the last century by selection from local wheat. Method of SDS-PAG electrophoresis according to Laemmli was used for fractionation of HMW glutenin subunits. Results. A total 11 alleles at the Glu-1 loci were identified, including 3 alleles at the Glu-A1 (a, b, c) and Glu-D1 (a, b, d) loci, and 5 – at the Glu- B1 (c, u, an, aj and subunit 9). Differences in frequencies of glutenin alleles were revealed. Conclusions. In the gene pool of Ukrainian winter bread wheat landraces the most widespread alleles were Glu-A1a (43.3 %), Glu-A1b (40.5 %), Glu-B1c (58 %), Glu-B1u (23 %), Glu-D1d (48.6 %), Glu-D1a (47.2 %). All these alleles (except of the Glu-D1a) are also predominant in the gene pool of modern commercial Ukrainian cultivars. A distinctive feature of Ukrainian landraces are the rare allelic variants of the Glu-B1 locus, which encode the subunits 1By9 and 1By8 (allele Glu-B1aj). Keywords: Triticum aestivum L., winter wheat, landraces, high-molecular-weight glutenin, alleles.

Variation and inheritance of cytosine methylation patterns in wheat at the high molecular weight glutenin and ribosomal RNA gene loci

Development ◽  
1990 ◽  
Vol 108 (Supplement) ◽  
pp. 15-20
Author(s):  
R. B. Flavell ◽  
M. O'Dell
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Cytosine Methylation ◽  
Seed Proteins ◽  
New Variant ◽  
Hmw Glutenin ◽  
Transcription Complexes ◽  
Methylation Patterns ◽  
Sexual Crosses ◽  
Rna Genes

Chromosome marking by cytosine methyiation has been examined in two gene systems in wheat – at the loci encoding high molecular weight (HMW) glutenin subunits (seed proteins) and ribosomai RNA. Variation in cytosine methyiation occurs between progeny in highly inbred lines around the HMW glutenin locus. The variation is inherited through meiosis to F1, and F2 generations but occasionally a new variant arises. Specific cytosine residues lose their methyl group in the seed, the organ where the genes are expressed. Within the multigene family of ribosomai RNA genes, several subsets of genes can be defined based upon the cytosine methylation patterns. High activity of a ribosomai RNA gene locus is correlated with loss of methylation at specific cytosine residues, especially in the promoter and upstream regulatory regions. A model is described in which the subset of genes selected to be used are those to which specific regulatory proteins and transcription complexes bind most favourably. Binding of such proteins inhibits cytosine methylation and so marks the subset of genes for expression in subsequent cell generations. Examples are described where new types of RNA genes are introduced via sexual crosses that result in changes to the methylation patterns of the ribosomai RNA genes. The processes determining the changes begin, it is believed, in the fertilised egg.

scholarly journals Conformational differences between two wheat (Triticum aestivum) ‘high-molecular-weight’ glutenin subunits are due to a short region containing six amino acid differences

1989 ◽  
Vol 263 (3) ◽  
pp. 837-842 ◽  
Author(s):  
A P Goldsbrough ◽  
N J Bulleid ◽  
R B Freedman ◽  
R B Flavell
Keyword(s):  
Molecular Weight ◽  
Triticum Aestivum ◽  
Amino Acid ◽  
High Molecular Weight ◽  
Polyacrylamide Gel Electrophoresis ◽  
Amino Acid Sequences ◽  
Glutenin Subunits ◽  
Sds Page ◽  
Hmw Glutenin

‘High-molecular-weight’ (HMW, high-Mr) glutenin subunits are protein constituents of wheat (Triticum aestivum) seeds and are responsible in part for the viscoelasticity of the dough used to make bread. Two subunits, numbered 10 and 12, are the products of allelic genes. Their amino acid sequences have been derived from the nucleic acid sequences of the respective genes. Subunit 10 has fewer amino acids than subunit 12, but migrates more slowly on SDS/PAGE (polyacrylamide-gel electrophoresis). This anomaly is due to between one and six of the amino acid differences between the subunits, localized towards the C-terminal end of the proteins. This has been established by making chimaeric genes between the genes for subunits 10 and 12, transcribing and translating them in vitro and analysing the products by SDS/PAGE. The postulated conformational differences between subunits 10 and 12 are discussed in relation to current hypotheses for the structure of HMW glutenin subunits.

Gel Entrapment of Antibody: A New Strategy for Facilitating Both Manual and Automated Radioimmunoassay

1973 ◽  
Vol 19 (12) ◽  
pp. 1339-1344 ◽  
Author(s):  
Stuart J Updike ◽  
John D Simmons ◽  
Douglas H Grant ◽  
Judith A Magnuson ◽  
Theodore L Goodfriend
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Room Temperature ◽  
Solid Phase ◽  
Binding Activity ◽  
Angiotensin I ◽  
Chromatographic Columns ◽  
New Strategy ◽  
Sample Application ◽  
Solid Phase Binding

Abstract A technique of radioimmunoassay is presented that eliminates pipetting and centrifugation, and excludes interferences by high-molecular-weight materials from the incubation and separation steps. A solid-phase binding reagent is prepared by first entrapping antibody in polyacrylamide gel. This gel is then fragmented, sieved, dried with ethanol or lyophilized, and placed in miniature disposable chromatographic columns. Application of the sample to the intra-gel column compartment is determined by the water regain of the gel. This pipetless method of sample application depends on reproducible aliquots of dry gel particles in every column. A method for preloading radiolabeled hormone and standard hormone into the column is also described. This technique has been successfully applied to the assay of angiotensin I and insulin. Dry antibody—gel stored at room temperature for 26 months has not shown loss of binding activity.

scholarly journals Molecular Characterization of Novel x-Type HMW Glutenin Subunit 1B × 6.5 in Wheat

Plants ◽  
2021 ◽  
Vol 10 (10) ◽  
pp. 2108
Author(s):  
Tímea Kuťka Hlozáková ◽  
Zdenka Gálová ◽  
Svetlana Šliková ◽  
Leona Leišová-Svobodová ◽  
Jana Beinhauer ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Molecular Characterization ◽  
Glutenin Subunit ◽  
Specific Primers ◽  
Sds Page ◽  
Hmw Glutenin ◽  
Sequence Encoding ◽  
High Level

A novel high molecular weight glutenin subunit encoded by the Glu-1B locus was identified in the French genotype Bagou, which we named 1B × 6.5. This subunit differed in SDS-PAGE from well-known 1B × 6 and 1B × 7 subunits, which are also encoded at this locus. Subunit 1B × 6.5 has a theoretical molecular weight of 88,322.83 Da, which is more mobile than 1B × 6 subunit, and isoelectric point (pI) of about 8.7, which is lower than that for 1B × 6 subunit. The specific primers were designed to amplify and sequence 2476 bp of the Glu-1B locus from genotype Bagou. A high level of similarity was found between the sequence encoding 1B × 6.5 and other x-type encoding alleles of this locus.

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