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1.
Mol Phylogenet Evol ; 175: 107591, 2022 10.
Article in English | MEDLINE | ID: mdl-35863609

ABSTRACT

Tracing evolutionary history proves challenging for polyploid groups that have evolved rapidly, especially if an ancestor of a polyploid is extinct. The Ns-containing polyploids are recognized as the NsXm and StHNsXm genomic constitutions in Triticeae. The Ns originated from Psathyrostachys, while the Xm represented a genome of unknown origin. Here, we use genetic information in plastome to trace the complex lineage history of the Ns-containing polyploid species by sampling 26 polyploids and 90 diploid taxa representing 23 basic genomes in Triticeae. Phylogenetic reconstruction, cluster plot of genetic distance matrix, and migration event demonstrated that (1) the Ns plastome originated from different Psathyrostachys species, and the Xm plastome may originate from an ancestral lineage of Henrardia, Agropyron, and Eremopyrum; (2) the Ns, Xm, and St genome donors separately served as the maternal parents during the speciation of the Ns-containing polyploid species, resulting in a maternal haplotype polymorphism; (3) North AmericanLeymusspecies might originate from colonization during late Miocene via the Bering land bridge and were the paternal donor of the StHNsXm genome Pascopyrum species. Our results shed new light on our understanding of the rich diversity and ecological adaptation of the Ns-containing polyploid species.


Subject(s)
Poaceae , Polyploidy , Biological Evolution , Genome, Plant , Phylogeny , Poaceae/genetics , Sequence Analysis, DNA
2.
J Sep Sci ; 37(24): 3760-6, 2014 Dec.
Article in English | MEDLINE | ID: mdl-25283274

ABSTRACT

Barley seedlings are rich in flavones that can have positive effects on people with antihypoxia and antifatigue. Lutonarin and saponarin are two major flavonoid glycosides that have unique structures in barley seedlings. This study presents a new approach for the preparation of lutonarin and saponarin from barely seedlings by membrane separation technology and preparative high-performance liquid chromatography. Preparative conditions of these two flavonoid glycosides by membrane separation technology were studied using response surface methodology. Under the optimized conditions, the total contents of these two flavonoid glycosides amounts to 17.0%.


Subject(s)
Apigenin/chemical synthesis , Apigenin/isolation & purification , Flavonoids/isolation & purification , Glucosides/chemical synthesis , Glucosides/isolation & purification , Glycosides/isolation & purification , Hordeum/chemistry , Seedlings/chemistry , Apigenin/chemistry , Chromatography, High Pressure Liquid , Flavonoids/chemical synthesis , Flavonoids/chemistry , Glucosides/chemistry , Glycosides/chemical synthesis , Glycosides/chemistry , Molecular Structure
3.
J Microbiol Biotechnol ; 18(7): 1245-51, 2008 Jul.
Article in English | MEDLINE | ID: mdl-18667852

ABSTRACT

Oxalate decarboxylases (OXDCs) (E.C. 4.1.1.2) are enzymes catalyzing the conversion of oxalate to formate and CO2 The OXDCs found in fungi and bacteria belong to functionally diverse protein superfamily known as the cupins. Fungi-originated OXDCs are secretory enzymes. However, most bacterial OXDCs are localized in the cytosol, and may be involved in energy metabolism. In Agrobacterium tumefaciens C58, a locus for a putative oxalate decarboxylase is present. In the study reported here, an enzyme was overexpressed in Escherichia coli and showed oxalate carboxylase activity. Computational analysis revealed the A. tumefaciens C58 OXDC contains a signal peptide mediating translocation of the enzyme into the periplasm that was supported by expression of signal-peptideless and full-length versions of the enzyme in A. tumefaciens C58. Further site-directed mutagenesis experiment demonstrated that the A. tumefaciens C58 OXDC is most likely translocated by a twin-arginine translocation (TAT) system.


Subject(s)
Agrobacterium tumefaciens/enzymology , Arginine/metabolism , Bacterial Proteins/metabolism , Carboxy-Lyases/metabolism , Protein Sorting Signals , Agrobacterium tumefaciens/chemistry , Agrobacterium tumefaciens/genetics , Agrobacterium tumefaciens/metabolism , Amino Acid Sequence , Bacterial Proteins/chemistry , Bacterial Proteins/genetics , Carboxy-Lyases/chemistry , Carboxy-Lyases/genetics , Escherichia coli/genetics , Escherichia coli/metabolism , Gene Expression , Molecular Sequence Data , Periplasm/chemistry , Periplasm/enzymology , Periplasm/genetics , Periplasm/metabolism , Protein Transport , Sequence Alignment
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