Sequence Analysis of the 5′-Terminal Part of GLU-D1 Locus of Landraces and Old Cultivars of Wheat (Triticum aestivum)

2000 ◽  
Vol 28 (4) ◽  
pp. 411-416
Author(s):  
J. Ovesná ◽  
S. Svobodová ◽  
I. Nováková ◽  
L. Dotlačil
Keyword(s):  
Triticum Aestivum ◽  
Sequence Analysis ◽  
Terminal Part

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 Emergence and subsequent functional specialization of kindlins during evolution of cell adhesiveness

2015 ◽  
Vol 26 (4) ◽  
pp. 786-796 ◽  
Author(s):  
Julia Meller ◽  
Igor B. Rogozin ◽  
Eugenia Poliakov ◽  
Nahum Meller ◽  
Mark Bedanov-Pack ◽  
...  
Keyword(s):  
Sequence Analysis ◽  
Functional Divergence ◽  
Focal Adhesions ◽  
Functional Specialization ◽  
Interacting Proteins ◽  
Ph Domain ◽  
Terminal Part ◽  
Encoding Gene ◽  
Sequence Encoding ◽  
Multicellular Organisms

Kindlins are integrin-interacting proteins essential for integrin-mediated cell adhesiveness. In this study, we focused on the evolutionary origin and functional specialization of kindlins as a part of the evolutionary adaptation of cell adhesive machinery. Database searches revealed that many members of the integrin machinery (including talin and integrins) existed before kindlin emergence in evolution. Among the analyzed species, all metazoan lineages—but none of the premetazoans—had at least one kindlin-encoding gene, whereas talin was present in several premetazoan lineages. Kindlin appears to originate from a duplication of the sequence encoding the N-terminal fragment of talin (the talin head domain) with a subsequent insertion of the PH domain of separate origin. Sequence analysis identified a member of the actin filament–associated protein 1 (AFAP1) superfamily as the most likely origin of the kindlin PH domain. The functional divergence between kindlin paralogues was assessed using the sequence swap (chimera) approach. Comparison of kindlin 2 (K2)/kindlin 3 (K3) chimeras revealed that the F2 subdomain, in particular its C-terminal part, is crucial for the differential functional properties of K2 and K3. The presence of this segment enables K2 but not K3 to localize to focal adhesions. Sequence analysis of the C-terminal part of the F2 subdomain of K3 suggests that insertion of a variable glycine-rich sequence in vertebrates contributed to the loss of constitutive K3 targeting to focal adhesions. Thus emergence and subsequent functional specialization of kindlins allowed multicellular organisms to develop additional tissue-specific adaptations of cell adhesiveness.

Triticum aestivum puroindolines, two basic cystine-rich seed proteins: cDNA sequence analysis and developmental gene expression

1994 ◽  
Vol 25 (1) ◽  
pp. 43-57 ◽  
Author(s):  
Marie-Fran�oise Gautier ◽  
Marie-Elisabeth Aleman ◽  
Anne Guirao ◽  
Didier Marion ◽  
Philippe Joudrier
Keyword(s):  
Gene Expression ◽  
Triticum Aestivum ◽  
Sequence Analysis ◽  
Cdna Sequence ◽  
Seed Proteins ◽  
Developmental Gene ◽  
Developmental Gene Expression ◽  
Cdna Sequence Analysis

scholarly journals Model for the phycobilisome rod with interlocking disks based on domain-weighted linker-polypeptide sequence homologies ofMastigocladus laminosus

2000 ◽  
Vol 2 (1) ◽  
pp. 31-40 ◽  
Author(s):  
Axel Parbel ◽  
Hugo Scheer
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Class Ii ◽  
Terminal Part ◽  
Amino Acid Sequence Analysis ◽  
X Ray ◽  
The Core ◽  
Sequence Homologies ◽  
Polypeptide Sequence

The 8 linker-polypeptides from the cyanobacteriumMastigocladus laminosuswere examined by comparative amino-acid sequence analysis for the predicted domain structure reported in the literatur (Glauser 1991, Esteban 1993) in detail using split sequences for the rod, rod-core and for the repeats from the core-membrane linker-polypeptide(Lcm127.6). This analysis gives two distinct domains, where domain 1 (∼22 kDa, identity between 31 and 70%) is present in the N-terminal two thirds of the class II linkers (∼30 kDa) and in the repeats of theLcm127.6, and domain 2 (∼10 kDa, identity between 28 and 41%) in the C-terminal part of the class II rod linkers (Lr31.5andLr32.5) and in the two capping linkers (Lc7.7andLr8.2). Based on these data, X-ray structure analysis from phycobiliproteins and proteolysis experiments, an interlocking model for the phycobilisome rod organization is proposed, with linkers protruding from one phycobilisome disk into the neighbouring one.

Ultrastructure of Plant Leaf Tissue Infected with Mite-Borne Viral-Like Pathogens

1970 ◽  
Vol 28 ◽  
pp. 178-179 ◽  
Author(s):  
O. E. Bradfute ◽  
R. E. Whitmoyer ◽  
L. R. Nault
Keyword(s):  
Triticum Aestivum ◽  
Zea Mays ◽  
Electron Microscope ◽  
Hordeum Vulgare ◽  
Microscope Study ◽  
Electron Microscope Study ◽  
Leaf Tissue ◽  
Leaf Ultrastructure ◽  
Double Membrane ◽  
Aceria Tulipae

A pathogen transmitted by the eriophyid mite, Aceria tulipae, infects a number of Gramineae producing symptoms similar to wheat spot mosaic virus (1). An electron microscope study of leaf ultrastructure from systemically infected Zea mays, Hordeum vulgare, and Triticum aestivum showed the presence of ovoid, double membrane bodies (0.1 - 0.2 microns) in the cytoplasm of parenchyma, phloem and epidermis cells (Fig. 1 ).

Phylogeny and taxonomy of the family Arthrodermataceae (dermatophytes) using sequence analysis of the ribosomal ITS region

1999 ◽  
Vol 37 (2) ◽  
pp. 105-114 ◽  
Author(s):  
Y. GRAser ◽  
M. EL Fari ◽  
R. Vilgalys ◽  
A. F. A. Kuijpers ◽  
G. S. DE Hoog ◽  
...  
Keyword(s):  
Sequence Analysis ◽  
Its Region ◽  
The Family
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