کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
4496032 1623834 2015 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Molecular characterization of the puroindoline-a and b alleles in synthetic hexaploid wheats and in silico functional and structural insights into Pina-D1
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک علوم کشاورزی و بیولوژیک (عمومی)
پیش نمایش صفحه اول مقاله
Molecular characterization of the puroindoline-a and b alleles in synthetic hexaploid wheats and in silico functional and structural insights into Pina-D1
چکیده انگلیسی


• Grain hardness is determined by tightly linked Puroindoline genes, Pina and Pinb.
• Three new Pina alleles were found and were designated as Pina-D1w, Pina-D1x and Pina-D1y.
• Most of the structural features of Pina were found conserved.
• In silico structural and functional characteristics of Pina-D1 were highlighted.
• PINA have binding capacity with small parts of prolamins causing celiac disease of human.

Kernel hardness determined by two tightly linked Puroindoline genes, Pina-D1 and Pinb-D1, located on chromosome 5DS define commercially important characteristics, uses, major grades and export markets of wheat. This study was conducted to characterize Pina-D1 and Pinb-D1 alleles, in fifteen synthetic hexaploid wheats (SHWs) and its relation with grain hardness. Additionally, in silico functional analyses of puroindoline-a protein was conducted for better understanding of their putative importance in grain quality. Six different Pina-D1 alleles were identified in the SHWs, of which three i.e. Pina-D1a, Pina-D1c and Pina-D1d were already known whereas the other three had new sequence polymorphisms and were designated as Pina-D1w, Pina-D1x and Pina-D1y. Three different Pinb-D1 alleles were identified which have been reported earlier and no novel sequence polymorphism was detected. It was concluded that despite some primary, secondary and 3D structure variations, ligand binding sites and disulfide bonds discrepancies, the main features of PINA, i.e. the tryptophan-rich domain, the cysteine backbone, the signal peptide and basic identity of the proteins were all conserved. In silico analysis showed that puroindolines having binding capacity with small parts of prolamins causing celiac disease of human, however their potential role is not obvious. Conclusively, the new Pina-D1 alleles with modest effect on grain hardness, and insight into their functional and structural characteristics are important findings and their putative role in celiac disease require further studies to validate.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Theoretical Biology - Volume 376, 7 July 2015, Pages 1–7
نویسندگان
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