scholarly journals The Allelic Diversity of the Gibberellin Signaling Pathway Genes in Aegilops tauschii Coss

Plants ◽  
2020 ◽  
Vol 9 (12) ◽  
pp. 1696
Author(s):  
Mikhail S. Bazhenov ◽  
Anastasiya G. Chernook ◽  
Nikolay P. Goncharov ◽  
Nadezhda N. Chikida ◽  
Mariya Kh. Belousova ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Signaling Pathway ◽  
Plant Height ◽  
Bread Wheat ◽  
Aegilops Tauschii ◽  
Wheat Varieties ◽  
Reduced Height ◽  
Gibberellin Signaling ◽  
New Alleles

Gibberellin-insensitive reduced height genes are widely spread in modern wheat varieties, making them resistant to lodging under conditions of intensive farming. However, the limited diversity of these genes present in wheat germplasm can limit the adaptability of newly created cultivars to the changing climate. The diversity of the gibberellin signaling pathway genes involved in plant height control—Reduced height 1 (Rht-D1), Gibberellin-insensitive dwarf 1 (Gid1-D) and Gibberellin-insensitive dwarf 2 (Gid2-D)—was studied in the diploid wild goatgrass Aegilops tauschii Coss., one of the ancestral species of the bread wheat (Triticum aestivum L.) and the donor of its D subgenome, using high-throughput sequencing. The examination of 24 Ae. tauschii accessions of different geographical origins revealed a large number of new alleles (haplotypes) not found in bread wheat varieties. Some of the detected polymorphisms lead to changes in the amino acid sequence of proteins. Four isoforms (amino acid sequence variants) were found for the RHT-D1 protein, and two isoforms—for the GID1 and GID2 proteins, each. An analysis of the co-occurrence frequencies of various isoforms of the three proteins showed that their combinations were not random in Ae. tauschii, which may indicate the functional significance of their differences. New alleles of the Rht-D1, Gid1-D, and Gid2-D genes are promising for introgression into bread wheat and studying their effect on plant height and adaptability.

GENOTYPIC AND PHENOTYPIC VARIABILITY, HERITABILITY AND PHENOTYPIC CORRELATION FOR YIELD AND YIELD COMPONENTS IN BREAD WHEAT VARIETIES

2001 ◽  
Vol 49 (3) ◽  
pp. 237-242 ◽  
Author(s):  
K. Z. Korkut ◽  
I. BAŞER ◽  
O. Bilgin
Keyword(s):  
Grain Yield ◽  
Plant Height ◽  
Bread Wheat ◽  
Yield Components ◽  
Phenotypic Variability ◽  
Kernel Weight ◽  
Phenotypic Correlation ◽  
Genotypic Variability ◽  
Wheat Varieties ◽  
Yield And Yield Components

This research was conducted to determine the effect of genetic and phenotypic variability on the yield and yield components of some bread wheat varieties over a period of four years (1995–1998). Experiments were established according to a completely randomised block design with three replicates in the Experimental Field of Tekirda đ Agricultural Faculty, Thrace University. In the present research, genotypic and phenotypic variability, heritability and phenotypic correlation coefficients were estimated for plant height, spike length, number of spikelets per spike, number of spikes per square metre, thousand kernel weight, test weight and grain yield per hectare. The results of data analyses showed that the highest genotypic variability was obtained for per hectare yield, whereas the highest phenotypic variability values were found for plant height, thousand kernel weight and grain yield. For plant height, thousand grain yield and test weight, the broad sense heritability coefficient was found to be the highest, while it was low for spike length, number of spikelets per spike and number of Key words: bread wheat, genotypic variability, phenotypic variability, heritability coefficient, phenotypic correlation, grain yield

scholarly journals Morphological, Physiological, and Biochemical Characterization of Drought-Tolerant Wheat (Triticum spp.) Varieties

2021 ◽  
Vol 2021 ◽  
pp. 1-12
Author(s):  
Alemayehu Tefera ◽  
Mulugeta Kebede ◽  
Kassu Tadesse ◽  
Tsegaye Getahun
Keyword(s):  
Water Stress ◽  
Plant Height ◽  
Bread Wheat ◽  
Biochemical Parameters ◽  
Agricultural Research ◽  
Field Capacity ◽  
Wheat Varieties ◽  
Triticum Spp ◽  
Relative Water ◽  
Physiological And Biochemical

Wheat is one of the most important cereal crops and extensively cultivated in wide ranges of altitudes in Ethiopia. With an alarming population growth in the era of climatic change, there is a need for further crop improvement for sustainable production. In this regard, the study was carried out at the Kulumsa Agricultural Research Center (KARC) in a rainout shelter to investigate the responses of durum and bread wheat varieties to soil water stress in terms of selected morphological, physiological, and biochemical parameters. The 2 factors were combined factorially and arranged in a randomized complete block design with 3 replications. The 12 wheat varieties, 6 bread wheat and other 6 durum wheat, were sown in pots under well-watered (100% field capacity) and water-stressed (30% field capacity) conditions. Results revealed that water stress resulted in 26%, 9%, 23%, 16%, and 11% reductions in plant height, spike length, number of spikelets spike−1, relative water, and chlorophyll contents, respectively. The tested wheat varieties under water stress produced 28% and 6% more proline content and total soluble sugar, respectively, as mitigation strategies against drought. Results further exhibited that wheat varieties significantly differed in all of the measured traits except for the plant height and relative water content. The present study verified that the biochemical parameters needs to be considered as better traits to select wheat (Triticum spp.) varieties for drought tolerance under water stress conditions.

scholarly journals CHARACTERIZATION OF PUTATIVE HEAT SHOCK TRANSCRIPTION FACTOR (Hsf2) GENE INVOLVED IN REGULATING THE EXPRESSION OF HSP90 IN WHEAT UNDER TERMINAL HEAT STRESS

2020 ◽  
Vol 8 (6) ◽  
pp. 765-773
Author(s):  
Kavita Dubey ◽  
◽  
Suneha Goswami ◽  
Narendra Kumar ◽  
Ranjeet R. Kumar ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Heat Stress ◽  
Amino Acid ◽  
Heat Shock ◽  
Amino Acid Sequence ◽  
Global Climate ◽  
Aegilops Tauschii ◽  
Transcript Abundance ◽  
Wheat Crop ◽  
Limited Information

Wheat, being staple food grain crop, is highly sensitive to heat stress. The effect is more evident under present threat of global climate change. Very limited information about heat-responsive transcription factor is known in wheat. A putative Heat Shock Factor (HSF) was cloned from wheat under HS. The gene was titled as Hsf2 (acc No. KP063542). The nucleotide sequence was found to be 1551 bp long with open reading frame (ORF) of 1125 bp (5’UTR of 213bp and 3’UTR of 213bp). The amino acid sequence showed the presence of HSF_ DNA binding domain having high degree of similarity (homology) with other HSF coding gene of related species (Aegilops tauschii with 95% homology and 100% homology with Chinese spring cultivar of Triticum aestivum). The protein was observed to be localized in the nucleus. Phosphorylation study showed the presence of phosphorylated threonine at seventeen sites in amino acid sequence. Expression analysis of Hsf2 showed maximum relative fold expression (2.04fold) in the leaves of HD2967 under HS, as compared to control. The transcript abundance was observed maximum in thermotolerant cv., as compared to thermo susceptible. Current study established positive correlation between the expression of Hsf2 and HSP90 under HS. Hsf2, being regulator of HSPs can be used as potential molecular marker for screening wheat germplasm for thermo tolerance. It will pave the way for the development of ‘climate-smart’ wheat crop.

scholarly journals Alleles of Ppd-D1 gene in the collection of Aegilops tauschii accessions and bread wheat varieties

2012 ◽  
Vol 28 (2) ◽  
pp. 149-155 ◽  
Author(s):  
G. O. Chebotar ◽  
S. V. Chebotar ◽  
D. O. Babenko ◽  
I. I. Motsnyy ◽  
A. B. Scherban ◽  
...  
Keyword(s):  
Bread Wheat ◽  
Aegilops Tauschii ◽  
Wheat Varieties

The staining pattern of the tropomyosin sequence is displayed in a new paracrystal

1986 ◽  
Vol 44 ◽  
pp. 150-151
Author(s):  
M.K. Lamvik ◽  
L.L. Klatt
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Staining Pattern ◽  
Banding Patterns ◽  
Mass Thickness ◽  
New Form

Tropomyosin paracrystals have been used extensively as test specimens and magnification standards due to their clear periodic banding patterns. The paracrystal type discovered by Ohtsuki1 has been of particular interest as a test of unstained specimens because of alternating bands that differ by 50% in mass thickness. While producing specimens of this type, we came across a new paracrystal form. Since this new form displays aligned tropomyosin molecules without the overlaps that are characteristic of the Ohtsuki-type paracrystal, it presents a staining pattern that corresponds to the amino acid sequence of the molecule.

Isolation and Structural Charaderization of a Potent Inhibitor of Coagulation Factor Xa from the Leech Haementeria ghilianii

1989 ◽  
Vol 61 (03) ◽  
pp. 437-441 ◽  
Author(s):  
Cindra Condra ◽  
Elka Nutt ◽  
Christopher J Petroski ◽  
Ellen Simpson ◽  
P A Friedman ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Salivary Gland ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Western Blot ◽  
Potent Inhibitor ◽  
Factor Xa ◽  
Coagulation Factor ◽  
Sds Page ◽  
Bovine Factor

SummaryThe present work reports the discovery and charactenzation of an anticoagulant protein in the salivary gland of the giant bloodsucking leech, H. ghilianii, which is a specific and potent inhibitor of coagulation factor Xa. The inhibitor, purified to homogeneity, displayed subnanomolar inhibition of bovine factor Xa and had a molecular weight of approximately 15,000 as deduced by denaturing SDS-PAGE. The amino acid sequence of the first 43 residues of the H. ghilianii derived inhibitor displayed a striking homology to antistasin, the recently described subnanomolar inhibitor of factor Xa isolated from the Mexican leech, H. officinalis. Antisera prepared to antistasin cross-reacted with the H. ghilianii protein in Western Blot analysis. These data indicate that the giant Amazonian leech, H. ghilianii, and the smaller Mexican leech, H. officinalrs, have similar proteins which disrupt the normal hemostatic clotting mechanisms in their mammalian host’s blood.

Paris I Dysfibrinogenemia: A Point Mutation in Intron 8 Results in Insertion of a 15 Amino Acid Sequence in the Fibrinogen γ-Chain

1993 ◽  
Vol 69 (03) ◽  
pp. 217-220 ◽  
Author(s):  
Jonathan B Rosenberg ◽  
Peter J Newman ◽  
Michael W Mosesson ◽  
Marie-Claude Guillin ◽  
David L Amrani
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Point Mutation ◽  
Genomic Dna ◽  
Comparative Sequence Analysis ◽  
Chain Gene ◽  
Molecular Defect ◽  
Nucleotide Position ◽  
Normal Individuals ◽  
Polymerase Chain

SummaryParis I dysfibrinogenemia results in the production of a fibrinogen molecule containing a functionally abnormal γ-chain. We determined the basis of the molecular defect using polymerase chain reaction (PCR) to amplify the γ-chain region of the Paris I subject’s genomic DNA. Comparative sequence analysis of cloned PCR segments of normal and Paris I genomic DNA revealed only an A→G point mutation occurring at nucleotide position 6588 within intron 8 of the Paris I γ-chain gene. We examined six normal individuals and found only normal sequence in this region, indicating that this change is not likely to represent a normal polymorphism. This nucleotide change leads to a 45 bp fragment being inserted between exons 8 and 9 in the mature γparis I chain mRNA, and encodes a 15 amino acid insert after γ350 [M-C-G-E-A-L-P-M-L-K-D-P-C-Y]. Alternative splicing of this region from intron 8 into the mature Paris I γ-chain mRNA also results after translation into a substitution of S for G at position γ351. Biochemical studies of 14C-iodoacetamide incorporation into disulfide-reduced Paris I and normal fibrinogen corroborated the molecular biologic predictions that two additional cysteine residues exist within the γpariS I chain. We conclude that the insertion of this amino acid sequence leads to a conformationallyaltered, and dysfunctional γ-chain in Paris I fibrinogen.

Complete Covalent Structure of Human Platelet Factor 4

1979 ◽  
Vol 42 (05) ◽  
pp. 1652-1660 ◽  
Author(s):  
Francis J Morgan ◽  
Geoffrey S Begg ◽  
Colin N Chesterman
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Platelet ◽  
Platelet Factor 4 ◽  
Platelet Factor ◽  
Disulphide Bonds ◽  
Covalent Structure

SummaryThe amino acid sequence of the subunit of human platelet factor 4 has been determined. Human platelet factor 4 consists of identical subunits containing 70 amino acids, each with a molecular weight of 7,756. The molecule contains no methionine, phenylalanine or tryptophan. The proposed amino acid sequence of PF4 is: Glu-Ala-Glu-Glu-Asp-Gly-Asp-Leu-Gln-Cys-Leu-Cys-Val-Lys-Thr-Thr-Ser- Gln-Val-Arg-Pro-Arg-His-Ile-Thr-Ser-Leu-Glu-Val-Ile-Lys-Ala-Gly-Pro-His-Cys-Pro-Thr-Ala-Gin- Leu-Ile-Ala-Thr-Leu-Lys-Asn-Gly-Arg-Lys-Ile-Cys-Leu-Asp-Leu-Gln-Ala-Pro-Leu-Tyr-Lys-Lys- Ile-Ile-Lys-Lys-Leu-Leu-Glu-Ser. From consideration of the homology with p-thromboglobulin, disulphide bonds between residues 10 and 36 and between residues 12 and 52 can be inferred.

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