scholarly journals Isolation, sequencing of the HvnHID gene and its role in the purple-grain colour development in Tibetan hulless barley

2021 ◽  
Author(s):  
Xiaohua Yao ◽  
Leping Su ◽  
Youhua Yao ◽  
Likun An ◽  
Yixiong Bai ◽  
...  
Keyword(s):  
Biosynthetic Pathway ◽  
Seed Colour ◽  
Hulless Barley ◽  
Reading Frame ◽  
Isoflavone Biosynthesis ◽  
Tibetan Hulless Barley ◽  
Colour Development ◽  
Black Seeds ◽  
Grain Colour ◽  
Important Basis

2-hydroxyisoflavanone dehydratase (HID) plays an important role in isoflavone biosynthesis. In this study, HID was isolated from the seeds of the purple-grained Tibetan hulless barley variety Nerumuzha and the white-grained variety Kunlun 10. The HvnHID gene includes the 981 bp open reading frame and encodes a protein of 327 amino acids. It has a typical Abhydrolase_3 domain (78–306) and belongs to the carboxylesterase (CXE) family of the Abhydrolase_3 (α/β hydrolase) superfamily. There are eight nucleotide differences in the HvnHID coding sequence and two amino acid differences (one in the Abhydrolase_3 domain) between Nerumuzha and Kunlun 10. The HvnHID of hulless barley has the closest relationship with the HID in Hordeum vulgare, and the most distant relationship in Panicum hallii. At the early-mid stage of the seed colour development, the HvnHID expression levels in the purple and black seeds were significantly higher than in the white and blue ones (P < 0.01). During the seed colour development of purple-grained hulless barley, the expression of the key genes (HvnF3'H, HvnDRF, HvnANT1, and HvnGT) in the anthocyanidin biosynthetic pathway increased significantly, while the HvnHID expression decreased significantly (P < 0.01). Thus, it is likely that HvnHID negatively regulates the anthocyanidin biosynthesis. This result provides an important basis for further study of the biological functions of HvnHID in the anthocyanidin biosynthetic pathway.

scholarly journals Qualitative and semi-quantitative assessment of anthocyanins in Tibetan hulless barley from different geographical locations by UPLC-QTOF-MS and their antioxidant capacities

2021 ◽  
Vol 19 (1) ◽  
pp. 1-8
Author(s):  
Tangwei Zhang ◽  
Jialin Ma ◽  
Xuelian Wu ◽  
Zhihua Hao ◽  
Ci Dun ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Antioxidant Activity ◽  
Quantitative Assessment ◽  
Ultra Performance Liquid Chromatography ◽  
Total Anthocyanin ◽  
Hulless Barley ◽  
Flight Mass Spectrometry ◽  
Antioxidant Capacities ◽  
Tibetan Hulless Barley ◽  
Geographical Locations

Abstract Tibetan hulless barley (“qingke” in Chinese) is a valuable food in Tibet. Purple qingke (PQK) and black qingke (BQK), two special pigmented types of hulless barley, have traditionally been widely cultivated and consumed in Tibet for thousands of years. The composition and contents of anthocyanins of two cultivars are unknown. This study aimed to explore the composition and contents of anthocyanins of two cultivars and their antioxidant capacities. Six anthocyanins were identified by ultra-performance liquid chromatography-quadrupole-time of flight mass spectrometry from barley, most of the anthocyanins were acylated by malonyl group. The total anthocyanin contents ranged from 141 to 2,304 μg/g in PQK and from 248.7 to 2902.9 μg/g in BQK. Furthermore, qingke has strong antioxidant activity against DPPH, ABTS˙+, and FRAP. Qingke may be useful for treating or preventing diseases caused by the overproduction of radicals.

Bioinfomatics Analysis of the Anthocyanidin synthase Gene in Tree Peony

2014 ◽  
Vol 1010-1012 ◽  
pp. 1181-1184
Author(s):  
Yan Zhao Zhang ◽  
Yan Wei Cheng ◽  
Hui Yuan Ya ◽  
Chao Yun ◽  
Jian Ming Han ◽  
...  
Keyword(s):  
Plant Species ◽  
Structure Prediction ◽  
Biosynthetic Pathway ◽  
Resistance Breeding ◽  
Flower Color ◽  
Anthocyanin Synthesis ◽  
Tree Peony ◽  
Reading Frame ◽  
Transcriptome Database ◽  
Color Modification

Anthocyanin mainly responsible for flowers color in many plant species, it also accumulated in response to lots of environmental stress to reduce the damage to plant cell. Anthocyanin synthesis (ANS) protein is an important synthetase participated in anthocyanin biosynthetic pathway. In this study, we isolated the PsANS gene from transcriptome database built by our previous study. The PsANS gene contain an 1050bp open reading frame encoding 349 amino acid, phylogenetic analysis revealed that PsANS was segrated into a group with ANS from others plant species. Secondary and thri-dimension structure prediction also revealed that it may have similar function with ANS in others plant species. The identified PsANS gene would be helpful for further research in flower color modification and resistance breeding.

Salicylic Acid Decreases the Levels of Dehydrin-Like Proteins in Tibetan Hulless Barley Leaves under Water Stress

2006 ◽  
Vol 61 (3-4) ◽  
pp. 245-250 ◽  
Author(s):  
Xin Sun ◽  
Shu Yuan ◽  
Hong-Hui Lin
Keyword(s):  
Salicylic Acid ◽  
Water Stress ◽  
Electrolyte Leakage ◽  
Oxidative Injury ◽  
Hulless Barley ◽  
Barley Leaves ◽  
Tibetan Hulless Barley

The effects of salicylic acid (SA) on the accumulation of dehydrins in leaves of Tibetan hulless barley seedlings under water stress were investigated. The results indicated that SA decreased the levels of the four dehydrin-like proteins induced by water stress. The concentrations of these dehydrin-like proteins increased under water stress. However, their levels in SA-pretreated seedlings were always lower than in those receiving only water stress. Our results also indicated that the levels of dehydrin-like proteins decreased as the SA concentration increased. In SA-pretreated seedlings, electrolyte leakage, MDA and H2O2 content were rather higher than in seedlings receiving only water stress. By these results, we suggest that lower levels of dehydrin-like proteins in seedlings with SA treatment may be due to the greater accumulation of H2O2 induced by SA, which causes more oxidative injury under water stress.

scholarly journals Isolation and functional expression of human COQ2, a gene encoding a polyprenyl transferase involved in the synthesis of CoQ

2004 ◽  
Vol 382 (2) ◽  
pp. 519-526 ◽  
Author(s):  
Margareta FORSGREN ◽  
Anneli ATTERSAND ◽  
Staffan LAKE ◽  
Jacob GRÜNLER ◽  
Ewa SWIEZEWSKA ◽  
...  
Keyword(s):  
Biosynthetic Pathway ◽  
Functional Expression ◽  
Human Muscle ◽  
Null Mutant ◽  
Human Homologue ◽  
Gene Encoding ◽  
Reading Frame ◽  
Human Enzyme ◽  
Liver Cdna Library ◽  
Mutant Cells

The COQ2 gene in Saccharomyces cerevisiae encodes a Coq2 (p-hydroxybenzoate:polyprenyl transferase), which is required in the biosynthetic pathway of CoQ (ubiquinone). This enzyme catalyses the prenylation of p-hydroxybenzoate with an all-trans polyprenyl group. We have isolated cDNA which we believe encodes the human homologue of COQ2 from a human muscle and liver cDNA library. The clone contained an open reading frame of length 1263 bp, which encodes a polypeptide that has sequence homology with the Coq2 homologues in yeast, bacteria and mammals. The human COQ2 gene, when expressed in yeast Coq2 null mutant cells, rescued the growth of this yeast strain in the absence of a non-fermentable carbon source and restored CoQ biosynthesis. However, the rate of CoQ biosynthesis in the rescued cells was lower when compared with that in cells rescued with the yeast COQ2 gene. CoQ formed when cells were incubated with labelled decaprenyl pyrophosphate and nonaprenyl pyrophosphate, showing that the human enzyme is active and that it participates in the biosynthesis of CoQ.

The complete chloroplast genome of Tibetan hulless barley

2015 ◽  
Vol 28 (3) ◽  
pp. 324-325 ◽  
Author(s):  
Quan Xing Zeng ◽  
Jun Hong Yuan ◽  
Lin Yu Wang ◽  
Jun Qi Xu ◽  
Tashi Nyima
Keyword(s):  
Chloroplast Genome ◽  
Complete Chloroplast Genome ◽  
Hulless Barley ◽  
Tibetan Hulless Barley

Increased L-Ornithine Production in Corynebacterium glutamicum by Overexpression of a Gene Encoding a Putative Aminotransferase

2015 ◽  
Vol 25 (1) ◽  
pp. 45-50 ◽  
Author(s):  
Dai-Joong Kim ◽  
Gui-Hye Hwang ◽  
Ji-Na Um ◽  
Jae-Yong Cho
Keyword(s):  
Biosynthetic Pathway ◽  
Gene Promoter ◽  
Open Reading Frame ◽  
Aminotransferase Activity ◽  
Wild Type ◽  
Gene Encoding ◽  
Reading Frame ◽  
Dehydrogenase Gene ◽  
Putative Aminotransferase ◽  
Combined Overexpression

Overexpression of the NCgl0462 open reading frame, encoding a class II aminotransferase, was studied in conjunction with other enzymes in <smlcap>L</smlcap>-ornithine biosynthesis in an <smlcap>L</smlcap>-ornithine-producing strain. Expression of the wild-type NCgl0462 open reading frame, which displayed aminotransferase activity, was amplified by placing it under the control of the glyceraldehyde 3-phosphate dehydrogenase gene promoter in the pEK0 plasmid and in the genome. <smlcap>L</smlcap>-Ornithine production in <i>Corynebacterium</i><i>glutamicum</i> SJC8260 harboring plasmid and the genomic NCgl0462 open reading frame was increased by 8.8 and 21.6%, respectively. In addition, the combined overexpression of the NCgl0462 open reading frame within the genome along with the mutated <smlcap>L</smlcap>-ornithine biosynthesis genes <i>(argCJBD)</i> placed in the pEK0 plasmid in <i>C</i>. <i>glutamicum</i> SJC8260 resulted in significant improvement in <smlcap>L</smlcap>-ornithine production (12.48 g/l for combined overexpression compared with 8.42 g/l for the control). These results suggest that overexpression of the aminotransferase-encoding NCgl0462 open reading frame plays an unequivocal role in the <smlcap>L</smlcap>-ornithine biosynthetic pathway, with overlapping substrate specificity in <i>C</i>. <i>glutamicum</i>.

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