Allelic diversity of high-molecular-weight glutenin protein subunits in natural populations of Dasypyrum villosum (L.) Candargy

1993 ◽  
Vol 86 (7) ◽  
pp. 851-858 ◽  
Author(s):  
G.-Y. Zhong ◽  
C.O. Qualset
Author(s):  
Kirushanthy Kajendran ◽  
Naduviladath Vishvanath Chandrasekharan ◽  
Chamari Madhu Hettiarachchi ◽  
Wijerupage Sandhya Sulochana Wijesundera

<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>


2021 ◽  
Vol 29 ◽  
pp. 111-116
Author(s):  
T. O. Sobko ◽  
G.M. Lisova ◽  
O.M. Blagodarova

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.


1971 ◽  
Vol 49 (4) ◽  
pp. 473-475 ◽  
Author(s):  
Tai-Wing Wu ◽  
K. G. Scrimgeour

Inosine-5′-phosphate (IMP) dehydrogenase has been purified to apparent homogeneity from extracts of Bacillus subtilis. The enzyme is inhibited by GMP in a complex manner which suggests cooperative interaction between protein subunits of IMP dehydrogenase. Several techniques have been used to desensitize the enzyme to inhibition by GMP. IMP dehydrogenase has a high molecular weight, and is composed of subunits each with a molecular weight of approximately 100 000. The properties of IMP dehydrogenase from B. subtilis are compatible with its being a regulatory enzyme in the biosynthesis of GMP from IMP.


1980 ◽  
Vol 33 (2) ◽  
pp. 221 ◽  
Author(s):  
GJ Lawrence ◽  
KW Shepherd

The high molecular weight glutenin protein subunits (those with apparent molecular weight in the range 80000 to 140000) of 98 wheat cultivars have been examined using a discontinuous gel-electrophoresis system. The number of bands present in each cultivar ranged from three to five and at least 34 different band patterns were observed. Examination of these patterns revealed that some bands, or band combinations, are mutually exclusive and that they can be assigned to three groups. In one group, two pairs of bands occur as alternatives and these bands are controlled by genes on chromosome 1D of wheat. In the second group, three possibilities occur with cultivars possessing either one of two single bands or neither band. These patterns are controlled by a gene or genes on chromosome 1A. In the third group nine patterns occur, four consisting of single bands and five consisting of a pair of bands. Four of these nine patterns have been shown to be controlled by genes on chromosome 1B. The variation detected in the glutenin subunits is useful for cultivar identification, has a bearing on our understanding of wheat evolution, and raises questions concerning the nature of this variation.


Author(s):  
Richard B. Vallee

Microtubules are involved in a number of forms of intracellular motility, including mitosis and bidirectional organelle transport. Purified microtubules from brain and other sources contain tubulin and a diversity of microtubule associated proteins (MAPs). Some of the high molecular weight MAPs - MAP 1A, 1B, 2A, and 2B - are long, fibrous molecules that serve as structural components of the cytamatrix. Three MAPs have recently been identified that show microtubule activated ATPase activity and produce force in association with microtubules. These proteins - kinesin, cytoplasmic dynein, and dynamin - are referred to as cytoplasmic motors. The latter two will be the subject of this talk.Cytoplasmic dynein was first identified as one of the high molecular weight brain MAPs, MAP 1C. It was determined to be structurally equivalent to ciliary and flagellar dynein, and to produce force toward the minus ends of microtubules, opposite to kinesin.


Sign in / Sign up

Export Citation Format

Share Document